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927 results on '"Marahiel, Mohamed A."'

1. Topoisomer Differentiation of Molecular Knots by FTICR MS: Lessons from Class II Lasso Peptides

Author

Zirah, Séverine, Afonso, Carlos, Linne, Uwe, Knappe, Thomas A, Marahiel, Mohamed A, Rebuffat, Sylvie, and Tabet, Jean-Claude

Subjects
Quantitative Biology - Biomolecules
Abstract

Lasso peptides constitute a class of bioactive peptides sharing a knotted structure where the C-terminal tail of the peptide is threaded through and trapped within an N-terminalmacrolactamring. The structural characterization of lasso structures and differentiation from their unthreaded topoisomers is not trivial and generally requires the use of complementary biochemical and spectroscopic methods. Here we investigated two antimicrobial peptides belonging to the class II lasso peptide family and their corresponding unthreaded topoisomers: microcin J25 (MccJ25), which is known to yield two-peptide product ions specific of the lasso structure under collisioninduced dissociation (CID), and capistruin, for which CID does not permit to unambiguously assign the lasso structure. The two pairs of topoisomers were analyzed by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR MS) upon CID, infrared multiple photon dissociation (IRMPD), and electron capture dissociation (ECD). CID and ECDspectra clearly permitted to differentiate MccJ25 from its non-lasso topoisomer MccJ25-Icm, while for capistruin, only ECD was informative and showed different extent of hydrogen migration (formation of c\bullet/z from c/z\bullet) for the threaded and unthreaded topoisomers. The ECD spectra of the triply-charged MccJ25 and MccJ25-lcm showed a series of radical b-type product ions {\eth}b0In{\TH}. We proposed that these ions are specific of cyclic-branched peptides and result from a dual c/z\bullet and y/b dissociation, in the ring and in the tail, respectively. This work shows the potentiality of ECD for structural characterization of peptide topoisomers, as well as the effect of conformation on hydrogen migration subsequent to electron capture.

Published
2011
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20. Communication Breakdown: Dissecting the COM Interfaces between the Subunits of Nonribosomal Peptide Synthetases

Author

Fage, Christopher D., primary, Kosol, Simone, additional, Jenner, Matthew, additional, Öster, Carl, additional, Gallo, Angelo, additional, Kaniusaite, Milda, additional, Steinbach, Roman, additional, Staniforth, Michael, additional, Stavros, Vasilios G., additional, Marahiel, Mohamed A., additional, Cryle, Max J., additional, and Lewandowski, Józef R., additional

Published
2021
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25. Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis

Author

Chillappagari, Shashi, Seubert, Andreas, Trip, Hein, Kuipers, Oscar P., Marahiel, Mohamed A., and Miethke, Marcus

Subjects
Iron in the body -- Physiological aspects, Homeostasis -- Research, Microbial metabolism -- Research, Bacillus subtilis -- Physiological aspects, Copper in the body -- Physiological aspects, Biological sciences
Abstract

Copper and iron are essential elements for cellular growth. Although bacteria have to overcome limitations of these metals by affine and selective uptake, excessive amounts of both metals are toxic for the cells. Here we investigated the influences of copper stress on iron homeostasis in Bacillus subtilis, and we present evidence that copper excess leads to imbalances of intracellular iron metabolism by disturbing assembly of iron-sulfur cofactors. Connections between copper and iron homeostasis were initially observed in microarray studies showing upregulation of Fur-dependent genes under conditions of copper excess. This effect was found to be relieved in a csoR mutant showing constitutive copper efflux. In contrast, stronger Fur-dependent gene induction was found in a copper efflux-deficient copA mutant. A significant induction of the PerR regulon was not observed under copper stress, indicating that oxidative stress did not play a major role under these conditions. Intracellular iron and copper quantification revealed that the total iron content was stable during different states of copper excess or efflux and hence that global iron limitation did not account for copper-dependent Fur derepression. Strikingly, the microarray data for copper stress revealed a broad effect on the expression of genes coding for iron-sulfur cluster biogenesis (suf genes) and associated pathways such as cysteine biosynthesis and genes coding for iron-sulfur cluster proteins. Since these effects suggested an interaction of copper and iron-sulfur cluster maturation, a mutant with a conditional mutation of sufU, encoding the essential iron-sulfur scaffold protein in B. subtilis, was assayed for copper sensitivity, and its growth was found to be highly susceptible to copper stress. Further, different intracellular levels of SufU were found to influence the strength of Fur-dependent gene expression. By investigating the influence of copper on cluster-loaded SufU in vitro, Cu(I) was found to destabilize the scaffolded cluster at submicromolar concentrations. Thus, by interfering with iron-sulfur cluster formation, copper stress leads to enhanced expression of cluster scaffold and target proteins as well as iron and sulfur acquisition pathways, suggesting a possible feedback strategy to reestablish cluster biogenesis. doi: 10.1128/JB.00058-10

Published
2010

26. SufU is an essential iron-sulfur cluster scaffold protein in Bacillus subtilis

Author

Albrecht, Alexander G., Netz, Daili J.A., Miethke, Marcus, Pierik, Antonio J., Burghaus, Olaf, Peuckert, Florian, Lill, Roland, and Marahiel, Mohamed A.

Subjects
Bacillus subtilis -- Physiological aspects, Bacterial proteins -- Chemical properties, Cysteine -- Physiological aspects, Biological sciences
Abstract

Bacteria use three distinct systems for iron-sulfur (Fe/S) cluster biogenesis: the ISC, SUF, and NIF machineries. The ISC and SUF systems are widely distributed, and many bacteria possess both of them. In Escherichia coli, ISC is the major and constitutive system, whereas SUF is induced under iron starvation and/or oxidative stress. Genomic analysis of the Fe/S cluster biosynthesis genes in Bacillus subtilis suggests that this bacterium's genome encodes only a SUF system consisting of a sufCDSUB gene cluster and a distant sufA gene. Mutant analysis of the putative Fe/S scaffold genes sufU and sufA revealed that sufU is essential for growth under minimal standard conditions, but not sufA. The drastic growth retardation of a conditional mutant depleted of SufU was coupled with a severe reduction of aconitase and succinate dehydrogenase activities in total-cell lysates, suggesting a crucial function of SufU in Fe/S protein biogenesis. Recombinant SufU was devoid of Fe/S clusters after aerobic purification. Upon in vitro reconstitution, SufU bound an Fe/S cluster with up to ~1.5 Fe and S per monomer. The assembled Fe/S cluster could be transferred from SufU to the apo form of isopropylmalate isomerase Leul, rapidly forming catalytically active [4Fe-4S]-containing holo-enzyme. In contrast to native SufU, its D43A variant carried a Fe/S cluster after aerobic purification, indicating that the cluster is stabilized by this mutation. Further, we show that apo-SufU is an activator of the cysteine desulfurase SufS by enhancing its activity about 40-fold in vitro. SufS-dependent formation of holo-SufU suggests that SufU functions as an Fe/S cluster scaffold protein tightly cooperating with the SufS cysteine desulfurase. doi: 10.1128/JB.01536-09

Published
2010

28. Copper acquisition is mediated by YcnJ and regulated by YcnK and CsoR in Bacillus subtilis

Author

Chillappagari, Shashi, Miethke, Marcus, Trip, Hein, Kuipers, Oscar P., and Marahiel, Mohamed A.

Subjects
Bacillus subtilis -- Physiological aspects, Bacillus subtilis -- Genetic aspects, Bacterial genetics -- Physiological aspects, Copper -- Physiological aspects, Biological sciences
Abstract

Copper is an essential cofactor for many enzymes, and at over a threshold level, it is toxic for all organisms. To understand the mechanisms underlying copper homeostasis of the gram-positive bacterium Bacillus subtilis, we have performed microarray studies under copper-limiting conditions. These studies revealed that the ycnJ gene encodes a protein that plays an important role in copper metabolism, as it shows a significant, eightfold upregulation under copper-limiting conditions and its disruption causes a growth-defective phenotype under copper deprivation as well as a reduced intracellular content of copper. Native gel shift experiments with the periplasmic N-terminal domain of the YcnJ membrane protein (135 residues) disclosed its strong affinity to Cu(II) ions in vitro. Inspection of the upstream sequence of ycnJ revealed that the ycnK gene encodes a putative transcriptional regulator, whose deletion caused an elevated expression of ycnJ, especially under conditions of copper excess. Further studies demonstrated that the recently identified copper efflux regulator CsoR also is involved in the regulation of ycnJ expression, leading to a new model for copper homeostasis in B. subtilis.

Published
2009

29. Structural basis for the selectivity of the external thioesterase of the surfactin synthetase

Author

Koglin, Alexander, Lohr, Frank, Bernhard, Frank, Rogov, Vladimir V., Frueh, Dominique P., Strieter, Eric R., Mofid, Mohammad R., Guntert, Peter, Wagner, Gerhard, Walsh, Christopher T., Marahiel, Mohamed A., and Dotsch, Volker

Subjects
Surface active agents -- Usage -- Research, Ligases -- Research -- Usage, Environmental issues, Science and technology, Zoology and wildlife conservation, Usage, Research
Abstract

Non-ribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) found in bacteria, fungi and plants use two different types of thioesterases for the production of highly active biological compounds (1,2). Type [...]

Published
2008

30. The major facilitator superfamily-type transporter YmfE and the multidrug-efflux activator Mta mediate bacillibactin secretion in Bacillus subtilis

Author

Miethke, Marcus, Schmidt, Sarah, and Marahiel, Mohamed A.

Subjects
Bacillus subtilis -- Genetic aspects, Gene expression -- Physiological aspects, Biological sciences
Abstract

High-affinity iron acquisition in Bacillus subtilis is mediated via the bacillibactin catechole siderophore pathway. Three of the four essential pathway steps, bacillibactin synthesis, Fe-bacillibactin uptake, and Fe-bacillibactin hydrolysis have been characterized previously. The functional and regulatory components for bacillibactin secretion, the second step of the siderophore pathway, remained unknown. In this study, the screening of a B. subtilis exporter mutant library led to the identification of the YmfE major facilitator superfamily (MFS)-type transporter as a target for bacillibactin export. Analysis of iron-limited ymfE mutant cultures displayed an eightfold reduced bacillibactin secretion and, on the other hand, a 25-fold increased secretion of the bacillibactin precursor 2,3-dihydroxybenzoate. Investigation of the regulatory aspect revealed that bacillibactin secretion is, in contrast to all other components of the pathway, independent of the ferric uptake repressor Fur. Indeed, the MerR-type transcriptional regulator Mta was found to activate both bacillibactin secretion and ymfE gene expression, exposing Mta as an additional regulatory member of the bacillibactin pathway.

Published
2008

31. Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes

Author

Kopp, Florian, Linne, Uwe, Oberthur, Markus, and Marahiel, Mohamed A.

Subjects
Epoxy compounds -- Chemical properties, Amides -- Chemical properties, Biosynthesis -- Analysis, Chemistry
Abstract

A new method is described by using an amide ligation reaction for the characterization of acyl carrier protein (ACP)-bound reaction intermediates. This novel method has characterized the ACP-mediated biosynthesis of the unique 2,3-epoxyhexanoyl moiety of calcium-dependent antibiotic (CDA), which has disclosed a new type of FAD-dependent oxidase HxcO with enoyl-ACP epoxidase activity, as well as a second enoyl-ACP epoxidase, HcmO.

Published
2008

33. Contributors

Author

Aalen, Reidunn B., primary, Abdel-Wahab, Yasser H.A., additional, Adams, Michael E., additional, Adan, Roger A.H., additional, Ahima, Rexford S., additional, Ahmed, Naima, additional, Al-Massadi, Omar, additional, Altstein, Miriam, additional, Anouar, Youssef, additional, Anselmi, Laura, additional, Ansorge, Siegfried, additional, Antcheva, Nikolinka, additional, Antonova-Koch, Yevgeniya, additional, Appel, Jon R., additional, Arik, Anam J., additional, Arter, Alison L., additional, Arvan, Peter, additional, Ashkenazi, Avraham, additional, Baas, P.W., additional, Bado, André, additional, Baird, Andrew, additional, Baiula, Monica, additional, Bakaletz, Lauren O., additional, Bakken, Earl E., additional, Balaskó, Márta, additional, Baldwin, Graham S., additional, Banks, William A., additional, Barra, Donatella, additional, Barson, Jessica R., additional, Basille, Magali, additional, Bauer, Natalie N., additional, Bedini, Andrea, additional, Beeton, Christine, additional, Begley, David J., additional, Beinfeld, Margery C., additional, Bendena, William G., additional, Benoit, Stephen C., additional, Bentov, Itay, additional, Bern, Howard, additional, Bierbaum, Gabriele, additional, Billington, Charles J., additional, Blasiak, Anna, additional, Block, Norman L., additional, Bloom, Stephen. R., additional, Bonney, Iwona, additional, Bowie, John H., additional, Boyd, Sunny K., additional, Brain, Susan D., additional, Brede, Dag A., additional, Broeck, Jozef Vanden, additional, Brown, Kelly L., additional, Brown, Mark R., additional, Bugni, James M., additional, Bundgaard, Jens R., additional, Burel, Delphine, additional, Butenko, Melinka A., additional, Call, Melissa J., additional, Calò, Girolamo, additional, Campbell, Duncan John, additional, Carlsson, Anna, additional, Carr, Daniel B., additional, Carraway, Robert E., additional, Carreira, Marcos C., additional, Casanueva, Felipe F., additional, Cassella, Sarah N., additional, Casson, Stuart A., additional, Castaño, Justo P., additional, Cebrat, Marek, additional, Chappe, Valerie, additional, Chatenet, David, additional, Chen, Keqiang, additional, Chen, Chen, additional, Chen, Longchuan, additional, Chen, Duan, additional, Cheng, Carrie Y.Y., additional, Cho, Sung Ki, additional, Chow, Billy K.C., additional, Christopoulos, Arthur, additional, Chu, Shijian, additional, Clarke, Iain J., additional, Coast, Geoffrey M., additional, Compere, Vincent, additional, Concepcion, Gisela P., additional, Cone, Roger D., additional, Conlon, J. Michael, additional, Cornélissen, Germaine, additional, Courel, Maité, additional, Couture, Réjean, additional, Cramer, W.A., additional, Croft, Nathan P., additional, Crujeiras, Ana B., additional, Cuttitta, Frank, additional, Cynis, Holger, additional, D’Acquisto, F., additional, Davis, Jon F., additional, Davis, Thomas P., additional, de La Serre, Claire Barbier, additional, de Lartigue, Guillaume, additional, de Lecea, Luis, additional, de Oliveira Santos, Marcelo, additional, De Waard, Michel, additional, Bolette Hartmann, Carolyn F. Deacon, additional, Delestre, Charlène, additional, Delgado, Mario, additional, Demuth, Hans-Ulrich, additional, Deng, Xiaoming, additional, Dharmawardhana, Palitha, additional, Di Cosmo, Anna, additional, Dias, Simoni Campos, additional, Dickerson, Jonathan W., additional, Diep, Dzung B., additional, Dircksen, H., additional, Dischinger, Jasmin, additional, do Rego, Jean-Claude, additional, Dobner, Paul R., additional, Dockray, Graham J., additional, Dores, Robert M., additional, Ducroc, Robert, additional, Dudek, Nadine L., additional, Dumont, Yvan, additional, Duraffourd, Celine, additional, Duterte-Boucher, Dominique, additional, Eberlé, Alex N., additional, Egleton, Richard D., additional, Eipper, Betty A., additional, Engel, Jorg B., additional, Englander, Ella W., additional, Epelbaum, Jacques, additional, Erlanson-Albertsson, Charlotte, additional, Evangelista, S., additional, Fagan, Karen A., additional, Farber, Joshua M., additional, Farkasfalvi, Klára, additional, Fekete, Csaba, additional, Flatt, Peter R., additional, Flower, R.J., additional, Forssmann, Wolf-Georg, additional, Fournier, Alain, additional, Foy, Kevin Chu, additional, Franco, Octávio Luiz, additional, Frenkel, Dan, additional, Fricker, Lloyd D., additional, de la Fuente-Núñez, César, additional, Fukuda, Hiroo, additional, Gäde, Gerd, additional, Galas, Ludovic, additional, Gallagher, Patricia E., additional, Gandolfo, Pierrick, additional, Garcia-Espinosa, Maria A., additional, García-Sanmartín, Josune, additional, Geary, Nori, additional, Geng, Hua, additional, Germano, Patrizia M., additional, Goetze, Jens P., additional, Gonzalez, Alexis A., additional, Gonzalez, Ana, additional, Gosnell, Blake A., additional, Goto, Katsutoshi, additional, Gourcerol, Guillaume, additional, Gozes, I., additional, Gracia-Navarro, Francisco, additional, Grayson, Bernadette E., additional, Greeley, George H., additional, Greenwald-Yarnell, Megan, additional, Gressens, Pierre, additional, Grider, John R., additional, Grünewald, Jan, additional, Guerreiro, Juliano R., additional, Guerrini, Remo, additional, Guida, Filomena, additional, Guilhaudis, Laure, additional, Guilmeau, Sandra, additional, Gundlach, Andrew L., additional, Gutkowska, Jolanta, additional, Hackbarth, Clifton, additional, Haim Ohana, Y., additional, Halberg, Franz, additional, Hallberg, Mathias, additional, Hamidi, Sayyed A., additional, Han, Song, additional, Han, Ji-Sheng, additional, Hancock, Robert E.W., additional, Haque, Samer-ul, additional, Hara-Nishimura, Ikuko, additional, Hariton, Aliza, additional, Hartsock, Wendy J., additional, Harvey, Alan L., additional, Hasunuma, Itaru, additional, Henning, Robert J., additional, Heppner, Kristy M., additional, Hertweck, Kate L., additional, Herzog, Herbert, additional, Higashiyama, Tetsuya, additional, Hinuma, Shuji, additional, Hippenstiel, Stefan, additional, Hirakawa, Yuki, additional, Hirose, Shuichi, additional, Hirsch, Jochen R., additional, Hocke, Andreas C., additional, Hodges, Robert S., additional, Hoffmann, Werner, additional, Hökfelt, Tomas, additional, Holst, Jens Juul, additional, Holzer, Peter, additional, Horodyski, Frank M., additional, Hosoda, Hiroshi, additional, Hou, Xiaowen, additional, Huffaker, Alisa, additional, Iijima, Norio, additional, Ikeuchi, Momoko, additional, Imperial, Julita S., additional, Improta, Giovanna, additional, Inui, Akio, additional, Irwin, Nigel, additional, Ishii, Munehiro, additional, Iturrioz, Xavier, additional, Ivanisevic, Ljubica, additional, Iwao, Hiroshi, additional, Iwata, Takeo, additional, Izumi, Yasukatsu, additional, Izumiyama, Hajime, additional, Jankowski, Marek, additional, Janssen, Tom, additional, Jégou, Sylvie, additional, Jensen, Robert T., additional, Jethwa, Preeti H., additional, Johannessen, Helene, additional, Johanson, Conrad, additional, Judkowski, Valeria, additional, Kaczmarek, Przemyslaw, additional, Kageyama, Haruaki, additional, Kakimoto, Tatsuo, additional, Kang, Ki Sung, additional, Kangawa, Kenji, additional, Kastin, Abba J., additional, Kato, Johji, additional, Kaumaya, Pravin T.P., additional, Keep, Richard F., additional, Kem, William R., additional, Khomenko, Tetyana, additional, Kikuyama, Sakae, additional, Kim, Young-Joon, additional, Kimura, Sadao, additional, King, Ross, additional, Kiptoo, Paul, additional, Kishimoto, Ichiro, additional, Kitamura, Kazuo, additional, Kluczyk, Alicja, additional, Kobori, Hiroyuki, additional, Kodama, Yosuke, additional, Kojima, Masayasu, additional, Kondo, Yuki, additional, Körner, Meike, additional, Kosson, Piotr, additional, Kotz, Catherine M., additional, Krishnan, Bhavani, additional, Kulseng, Bård, additional, Kumpf, Robert, additional, Laburthe, Marc, additional, Lacaille, Hélène, additional, Ladenheim, Ellen E., additional, Ladram, Ali, additional, Laksitorini, Marlyn D., additional, Lambert, David G., additional, Lange, Angela B., additional, Langhans, Wolfgang, additional, Larauche, Muriel, additional, Larhammar, Dan, additional, Larráyoz, Ignacio M., additional, Lattanzi, Roberta, additional, Lechan, Ronald M., additional, Lefranc, Benjamin, additional, Leibowitz, Sarah F., additional, Lelièvre, Vincent, additional, Leprince, Jérôme, additional, Levine, Allen S., additional, Li, Qun, additional, Lifshitz, Veronica, additional, Lihrmann, Isabelle, additional, Chi-Jen Lin, James, additional, Lindberg, Iris, additional, Lindsey, Keith, additional, Lipkowski, Andrzej W., additional, Liron, T., additional, Liu, Junli, additional, Liu, Ying, additional, Liu, Min, additional, Llorens-Cortes, Catherine, additional, Loizidou, Marilena, additional, Lopez, C., additional, Lovejoy, David A., additional, Luca, Vincenzo, additional, Lutz, Thomas A., additional, Ma, Sherie, additional, Mains, Richard E., additional, Malagon, Maria M., additional, Malendowicz, Ludwik K., additional, Wan, Jennifer Man-Fan, additional, Mangoni, Maria Luisa, additional, Manigrasso, Michaele B, additional, Marahiel, Mohamed A., additional, Marco, Heather G., additional, Maric-Bilkan, Christine, additional, Marks, Nikki J., additional, Martin, Roland, additional, Martinez, Vicente, additional, Martínez, Alfredo, additional, Martinez-Fuentes, Antonio J., additional, Masler, Edward P., additional, Matsubayashi, Yoshikatsu, additional, Mattu, Harman S., additional, Maule, Aaron G., additional, McLaughlin, Patricia J., additional, McMurtry, Ivan F., additional, Meelkop, Ellen, additional, Mehdi, Saher, additional, Melchiorri, Pietro, additional, Millar, R.P., additional, Miller, Laurence J., additional, Miller, Miles, additional, Million, Mulugeta, additional, Minamino, Naoto, additional, Mittelman, M., additional, Miyauchi, Takashi, additional, Miyazato, Mikiya, additional, Mizoguchi, Hirokazu, additional, Mohme, Malte, additional, Montero-Hadjadje, Maité, additional, Moody, Terry W., additional, Mookherjee, Neeloffer, additional, Moran, Timothy H., additional, Morganstern, Irene, additional, Mori, Masatomo, additional, Morin, Fabrice, additional, Morris, John F., additional, Moura, Daniel S., additional, Mudge, Anna J., additional, Mul, Joram D., additional, Murthy, Karnam S., additional, Myers, Martin G., additional, Nachman, Ronald J., additional, Nahon, Jean-Louis, additional, Naithani, Sushma, additional, Nakada, Tomoaki, additional, Nakamachi, Tomoya, additional, Nakamura, Yuki, additional, Nalivaeva, Natalia N., additional, Nasrallah, June B., additional, Nässel, Dick R., additional, Navar, L. Gabriel, additional, Neelakantan, Pratap, additional, Negri, Lucia, additional, Nes, Ingolf F., additional, Neumann, D., additional, Neveu, Cindy, additional, Ng, Tzi Bun, additional, Ng, Stephanie Y.L., additional, Nicholson, Graham M., additional, Nicolas, Pierre, additional, Nishikimi, Toshio, additional, Nishiyama, Mariko, additional, Nogueiras, Rubén, additional, Norton, Raymond S., additional, Novotny, Laura A., additional, Nowak, Krzysztof W., additional, Nyberg, Fred, additional, Ochoa-Callejero, Laura, additional, Ove Ögren, Sven, additional, Ohgusu, Hideko, additional, Oh-I, Shinsuke, additional, Ojo, Opeolu O., additional, Olivera, Baldomero M., additional, Olucha-Bordonau, Francisco E., additional, Oppenheim, Joost J., additional, Orchard, Ian, additional, Ouellette, André J., additional, Pacheco-López, Gustavo, additional, Page, Nigel M., additional, Palma, Mario Sergio, additional, Pan, Weihong, additional, Park, Yoonseong, additional, Parmentier, Marc, additional, Passemard, Sandrine, additional, Patterson, Michael, additional, Paunovic, Brankica, additional, Pearce, Gregory, additional, Pedersen, Jens, additional, Peeters, Theo L., additional, Eugene Pekary, A., additional, Pelletier, Georges, additional, Perboni, Simona, additional, Pérez-Tilve, Diego, additional, Perjés, Ábel, additional, Perretti, M., additional, Pétervári, Erika, additional, Pinilla, Clemencia, additional, Pinskim, Jacek, additional, Pisegna, Joseph R., additional, Plankensteiner, Kristof, additional, Podvin, Sonia, additional, Poitras, Pierre, additional, Polese, Gianluca, additional, Pollock, David M., additional, Porto, William Farias, additional, Possani, Lourival D., additional, Pothoulakis, Charalabos, additional, Presse, Françoise, additional, Prieto, Minolfa C., additional, Prutchi-Sagiv, S., additional, Purcell, Anthony W., additional, Purtell, Louise, additional, Quirion, Rémi, additional, Rabat, Catalina Abad, additional, Rademaker, Miriam, additional, Rajpal, Gautam, additional, Randeva, Harpal S., additional, Rebuffat, Sylvie, additional, Reeve, Joseph R., additional, Rehfeld, Jens F., additional, Reinhold, Dirk, additional, Reinscheid, Rainer K., additional, Reubi, Jean Claude, additional, Rezvani, Katayoun, additional, Ribeiro, Suzana Meira, additional, Richard, D., additional, Richards, Mark, additional, Riehle, Michael A., additional, Rinaldi, Andrea C., additional, Rode, Bernd M., additional, de la Vega, Ricardo C. Rodríguez, additional, Rotzinger, Susan, additional, Rucinski, Marcin, additional, Ruskoaho, Heikki, additional, Ryan, Philip J., additional, Sabatier, Jean-Marc, additional, Sahl, Hans-Georg, additional, Said, Sami I., additional, Sakurada, Tsukasa, additional, Sakurada, Shinobu, additional, Salomon, David S., additional, Samson, Willis K., additional, Sandor, Zsuzsanna, additional, Saragovi, H. Uri, additional, Sasaki, Kazuki, additional, Sato, Takahiro, additional, Satou, Ryousuke, additional, Sawa, Shinichiro, additional, Sayegh, Ayman I., additional, Schally, Andrew V., additional, Schilling, Stephan, additional, Schoofs, Liliane, additional, Schooley, David A., additional, Schubert, Mitchell L., additional, Segalas-Milazzo, Isabelle, additional, Seidah, Nabil G., additional, Selsted, Michael E., additional, Seroogy, Kim B., additional, Severini, Cinzia, additional, Sexton, Patrick M., additional, Shai, Yechiel, additional, Sharma, O., additional, Shichiri, Masayoshi, additional, Shimada, Tomoo, additional, Shimizu, Hiroyuki, additional, Shioda, Seiji, additional, Shulkes, Arthur, additional, Siahaan, Teruna J., additional, Siemion, Ignacy Z., additional, Silva, Osmar Nascimento, additional, Silva-Filho, Marcio C., additional, Skwarczynski, Mariusz, additional, Small, Caroline. J., additional, Smith, Craig M., additional, Smith, David E., additional, Smith, A. Ian, additional, Solomon, Beka, additional, Solomon, Travis E., additional, Sospedra, Mireia, additional, Souroujon, M.C., additional, Spampinato, Santi, additional, Spindel, Eliot R., additional, Steiger, A., additional, Stengel, Andreas, additional, Sternini, Catia, additional, Steyn, Frederik J., additional, Stopa, Edward, additional, Strowski, Mathias Z., additional, Sugano, Shigeo S., additional, Sundström, Görel, additional, Sutcliffe, J. Gregor, additional, Suttorp, Norbert, additional, Sweedler, Jonathan V., additional, Szabo, Sandor, additional, Székely, Miklós, additional, Szokodi, István, additional, Taché, Yvette, additional, Takahashi, Kazuhiro, additional, Takei, Yoshio, additional, Takenoya, Fumiko, additional, Talbot, Sébastien, additional, Tallant, E. Ann, additional, Tan, Tricia M., additional, Temmerman, Liesbet, additional, Temmesfeld-Wollbrück, Bettina, additional, Tena-Sempere, Manuel, additional, Thorsell, Annika, additional, Tilakaratne, Nanda, additional, Tobe, Stephen S., additional, Tokudome, Takeshi, additional, Tolstanova, Ganna, additional, Tonon, Marie-Christine, additional, Topping, Jennifer F., additional, Tossi, Alessandro, additional, Tostivint, Hervé, additional, Toth, Istvan, additional, Totsune, Kazuhito, additional, Toyoda, Fumiyo, additional, Troke, Rachel, additional, Tschöp, Matthias H., additional, Tso, Patrick, additional, Tsukaya, Hirokazu, additional, Tsutsui, Kazuyoshi, additional, Tu, Hong, additional, Turner, Anthony J., additional, Ubuka, Takayoshi, additional, Valdivia, Elene R., additional, Vandersmissen, Hans Peter, additional, Vaudry, David, additional, Vaudry, Hubert, additional, Vazquez-Martinez, Rafael, additional, Verbalis, Joseph G., additional, Vicari, Daniele, additional, Vidal, Nicolas, additional, Vignoni, Marzia, additional, Viollet, Cécile, additional, Vishwanatha, K.S., additional, Vivoli, Mirella, additional, Voisin, Thierry, additional, Vu, John P., additional, Walker, John C., additional, Wallace, B.A., additional, Wang, Ji Ming, additional, Wang, Lixin, additional, Wardman, Jonathan H., additional, Watanabe, Takuya, additional, Welch, Hazel, additional, Werner, Haim, additional, Whitmore, L., additional, Wiedemann, Imke, additional, Winsky-Sommerer, Raphaelle, additional, Witt, Ken A., additional, Wojciechowicz, Tatiana, additional, Wong, Jack Ho, additional, Woods, Stephen C., additional, Wootten, Denise, additional, Wu, Vincent, additional, Wurtz, Olivier, additional, Xiong, Ximing, additional, David Xu, Zhi-Qing, additional, Yamaguchi, Yube, additional, Yamaguchi, Takahiro, additional, Yamamoto, Kazutoshi, additional, Yamashita, E., additional, Yamazaki, Hiroyuki, additional, Yang, De, additional, Yoshikawa, Masaaki, additional, Yuan, Pu-Qing, additional, Yung, Sunny C., additional, Zagon, Ian S., additional, Zakharov, S.D., additional, Zaman, Mehfuz, additional, Zhalnina, M.V., additional, Zhang, Ning, additional, Zhang-Auberson, Lixin, additional, Zhao, Chun-Mei, additional, Ziolkowska, Agnieszka, additional, and Zitnan, Dusan, additional

Published
2013
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34. Rational design of bacitracin A derivatives by incorporating natural product derived heterocycles

Author

Wagner, Bjorn, Schumann, Dirk, Linne, Uwe, Koert, Ulrich, and Marahiel, Mohamed A.

Subjects
Bacitracin -- Research, Peptides -- Research, Chemistry
Abstract

A method to selectively alter the heterocyclic metal binding subunit of Bacitracin A by the synthesis of heterocyclic building blocks that were successfully coupled to the linear decapeptide and subsequently cyclized using the excised bacitracin PCP-TE bidomain is described. The generated bacitracin derivatives showed bacterial activity, indicating the possibility of altering the biological important heterocyclic subunit and overcoming existing limitations for the application of bacitracin.

Published
2006

35. Identification of a gene cluster for biosynthesis of Mannosylerythritol lipids in the basidiomycetous fungus Ustilago maydis

Author

Hewald, Sandra, Linne, Uwe, Scherer, Mario, Marahiel, Mohamed A., Kamper, Jorg, and Bolker, Michael

Subjects
Basidiomycota -- Genetic aspects, Surface active agents -- Chemical properties, DNA microarrays -- Research, Biological sciences
Abstract

The identification of a gene cluster for mannosylerythritol lipid (MEL) biosynthesis, which consists of five open reading frames, is described. The mutation analysis demonstrates that putative acyltransferases Mac1 and Mac2 are essential for MEL biosynthesis and acetyltransferase Mat1 catalyzes the acetylation of mannosylerythritol lipids in Ustilago maydis.

Published
2006

36. Sigma L is important for cold shock adaptation of Bacillus subtilis

Author

Wiegeshoff, Frank, Beckering, Carsten L., Debarbouille, Michel, and Marahiel, Mohamed A.

Subjects
Bacillus subtilis -- Genetic aspects, Genetic transcription -- Research, Genetic research, Biological sciences
Abstract

Although sigma factor-dependent transcriptional regulation was shown to be essential for adaptation to different environmental stimuli, no such sigma factor has been related to the regulation of the cold shock response in Bacillus subtilis. In this study, we present genetic evidence for participation of [[delta].sup.L] ([[delta].sup.54]) and the two [[delta].sup.L]-dependent transcriptional enhancers BkdR and YplP in the cold shock response of Bacillus subtilis JH642. Single-gene deletion of either sigL, bkdR, or yplP resulted in a cold-sensitive phenotype.

Published
2006

37. Chemoenzymatic and template-directed synthesis of bioactive macrocyclic peptides

Author

Grunewald, Jan and Marahiel, Mohamed A.

Subjects
Peptides -- Chemical properties, Immunosuppressive agents -- Chemical properties, Enzyme activation -- Research, Biological sciences
Abstract

Non-ribosomally synthesized peptides have compelling biological activities ranging from antimicrobial to immunosuppressive and from cytostatic to antitumor. The broad spectrum of applications in modern medicine is reflected in the great structural diversity of these natural products and they contain unique building blocks, such as D-amino acids, fatty acids, sugar moieties, and heterocyclic elements, as well as, halogenated, methylated, and formylated residues.

Published
2006

38. Cold-induced putative DEAD box RNA helicases CshA and CshB are essential for cold adaptation and interact with cold shock protein B in Bacillus subtilis

Author

Hunger, Karen, Beckering, Carsten L., Wiegeshoff, Frank, Graumann, Peter L., and Marahiel, Mohamed A.

Subjects
Bacillus subtilis -- Genetic aspects, Bacillus subtilis -- Research, DNA-ligand interactions -- Research, Fluorescence microscopy -- Analysis, Biological sciences
Abstract

The nucleic acid binding cold shock proteins (CSPs) and the cold-induced DEAD box RNA helicases have been proposed separately to act as RNA chaperones, but no experimental evidence has been reported on a direct cooperation. To investigate the possible interaction of the putative RNA helicases CshA and CshB and the CSPs from Bacillus subtilis during cold shock, we performed genetic as well as fluorescence resonance energy transfer (FRET) experiments. Both cshA and cshB genes could be deleted only in the presence of a cshB copy in trans, showing that the presence of one csh gene is essential for viability. The combined gene deletion of cshB and cspD resulted in a cold-sensitive phenotype that was not observed for either helicase or csp single mutants. In addition to the colocalization of the putative helicases CshA and CshB with CspB and the ribosomes in areas surrounding the nucleoid, we detected a strong FRET interaction in vivo between CshB and CspB that depended on active transcription. In contrast, a FRET interaction was not observed for CshB and the ribosomal protein L1. Therefore, we propose a model in which the putative cold-induced helicases and the CSPs work in conjunction to rescue misfolded mRNA molecules and maintain proper initiation of translation at low temperatures in B. subtilis.

Published
2006

39. Biosynthesis of nonribosomal peptides

Author

Finking, Robert and Marahiel, Mohamed A.

Subjects
Biosynthesis -- Research, Peptides -- Synthesis, Peptides -- Research, Biological sciences
Abstract

The structure-function relationship of the core- and tailoring-domains of nonribosomal peptide synthetases (NRPSs) is reviewed and different biosynthetic strategies and essential enzymes for posttranslational modification and editing are discussed. It is found that several crystal structures of NRPS-domains have yielded deep insight into the catalytic mechanisms involved and have led to a better prediction of the products assembled and to the construction of hybrid enzymes.

Published
2004

40. Loading a peptidyl-coenzyme A onto peptidyl carrier proteins: A novel approach in characterizing macrocyclization by thioesterase domains

Author

Sieber, Stephan A., Walsh, Christopher T., and Marahiel, Mohamed A.

Subjects
Amines -- Chemical properties, Ring formation (Chemistry) -- Methods, Coenzymes -- Chemical properties, Esterases -- Chemical properties, Chemistry
Abstract

A new experimental approach is reported to characterize recombinant nonribosomal peptide cyclasses that do not show activity with conventional N-acetylcysteamine (SNAC) substrates. The regioselectivity of branched-chain cyclization catalyzed by the fengycin cyclase is characterized, which displays no activity with peptidyl SNAC substrates.

Published
2003

42. Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase

Author

Tseng, Claire C., Bruner, Steven D., Kohli, Rahul M., Marahiel, Mohamed A., Walsh, Christopher T., and Sieber, Stephan A.

Subjects
Biochemistry -- Research, Peptides -- Physiological aspects, Esters -- Physiological aspects, Enzymes -- Physiological aspects, Chemical inhibitors -- Physiological aspects, Chemical inhibitors -- Composition, Biological sciences, Chemistry
Abstract

Research has been conducted on the lipopeptide surfactin produced by the gram positive bacterium Bacillus subtilis. The cocrystal structures this lipopeptide with dipeptidyl boranate inhibitors have been studied and the results indicate that surfactin's cyclization conformation has been modeled into the enzyme active site.

Published
2002

43. Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics

Author

Eppelmann, Katrin, Stachelhaus, Torsten, and Marahiel, Mohamed A.

Subjects
Biochemistry -- Research, Peptides -- Physiological aspects, Antibiotics -- Physiological aspects, Phenylalanine -- Physiological aspects, Amino acids -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the nonribosomal peptides. The selectivity-conferring code of these peptides has been investigated in the attempt to alter their substrate selectivity both in vivo and in vitro and the details are presented.

Published
2002

44. Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase

Author

Luo, Lusong, Kohli, Raul M., Onishi, Meguni, Linne, Uwe, Marahiel, Mohamed A., and Walsh, Christopher T.

Subjects
Biochemistry -- Research, Peptides -- Physiological aspects, Esters -- Physiological aspects, Enzymes -- Physiological aspects, Cyclic compounds -- Physiological aspects, Antibiotics -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the cyclic decapeptide antibiotic tyrocidine. The evaluation of the three- and four-domain versions of the tyrocidine synthetase B module has been carried out via the use of the rapid quench techniques in investigating the ability of the module's domain to epimerise aminoacyl thioester and dipeptidyl-S-enzyme and the details are discussed.

Published
2002

46. Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases

Author

Linne, Uwe, Doekel, Sascha, and Marahiel, Mohamed A.

Subjects
Peptides -- Synthesis, Ligases -- Analysis, Polypeptides -- Analysis, Protein biosynthesis -- Research, Domain structure -- Analysis, Biological sciences, Chemistry
Abstract

Research reveals that epimerization domains are functionally portable to A domains, which epimerize altered substrates to synthesize nonribosomal peptide synthetases. Data suggest that epimerization activity requires the presence of peptidyl carrier protein domain or T domain.

Published
2001

47. Complementation of cold shock proteins by translation initiation factor IF1 in vivo

Author

Weber, Michael H.W., Beckering, Carsten L., and Marahiel, Mohamed A.

Subjects
Heat shock proteins -- Genetic aspects, Genetic translation -- Physiological aspects, Gene expression -- Analysis, Escherichia coli -- Genetic aspects, Bacillus subtilis -- Genetic aspects, Biological sciences
Abstract

Research demonstrates that heterologous expression of the Escherichia coli translation initiation factor IF1 in a Bacillus subtilis cold shock domain mutant strain, cures both the growth and sporulation defects in the mutant. Data suggest that IF1 and cold shock domain possess overlapping cellular functions.

Published
2001

48. Localization of cold shock proteins to cytosolic spaces surrounding nucleoids in Bacillus subtilis depends on active transcription

Author

Weber, Michael H. W., Volkov, Arsen V., Fricke, Ingo, Marahiel, Mohamed A., and Graumann, Peter L.

Subjects
Bacteriology -- Research, Proteins -- Analysis, Cytosol -- Physiological aspects, Bacillus subtilis -- Genetic aspects, Genetic transcription -- Physiological aspects, Cells -- Growth, Immunofluorescence -- Usage, Biological sciences
Abstract

Research has been conducted on the cold shock proteins. The results of the immunofluorescence microscopy and fusion of the cold shock protein to the green fluorescent protein indicate that cold shock proteins localize to the cytosolic regions surrounding the nucleoid in the Bacillus subtilis growing cells.

Published
2001

49. Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases

Author

Kohli, Rahul M., Trauger, John W., Schwarzer, Dirk, Marahiel, Mohamed A., and Walsh, Christopher T.

Subjects
Peptides -- Research, Ring formation (Chemistry) -- Analysis, Structure-activity relationships (Biochemistry) -- Analysis, Domain structure -- Analysis, Biological sciences, Chemistry
Abstract

Results indicate that cyclization of acyl thioester substrates, catalyzed by thioesterase domains of nonribosomal peptide synthetase, yield diverse biologically active molecules. Solid-phase synthesis and thioesterase-mediated cyclization of linear peptide thioesters are discussed.

Published
2001

50. Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase

Author

Trauger, John W., Kohli, Rahul M., Mootz, Henning D., Marahiel, Mohamed A., and Walsh, Christopher T.

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): John W. Trauger [1]; Rahul M. Kohli [1]; Henning D. Mootz [2]; Mohamed A. Marahiel [2]; Christopher T. Walsh (corresponding author) [1] In the biosynthesis of many macrocyclic natural [...]

Published
2000
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