18 results on '"Stewart, A. Francis"'
Search Results
2. Gene Targeting and Site-Specific Recombination in Mouse ES Cells
- Author
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Anastassiadis, Konstantinos, primary, Schnütgen, Frank, additional, von Melchner, Harald, additional, and Stewart, A. Francis, additional
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- 2013
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3. A Practical Summary of Site-Specific Recombination, Conditional Mutagenesis, and Tamoxifen Induction of CreERT2
- Author
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Anastassiadis, Konstantinos, primary, Glaser, Stefan, additional, Kranz, Andrea, additional, Bernhardt, Kaj, additional, and Stewart, A. Francis, additional
- Published
- 2010
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4. A Recombineering Pipeline to Make Conditional Targeting Constructs
- Author
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Fu, Jun, primary, Teucher, Madeleine, additional, Anastassiadis, Konstantinos, additional, Skarnes, William, additional, and Stewart, A. Francis, additional
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- 2010
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5. Engineering Embryonic Stem Cells with Recombinase Systems
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Schnütgen, Frank, primary, Stewart, A. Francis, additional, von Melchner, Harald, additional, and Anastassiadis, Konstantinos, additional
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- 2006
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6. Engineering of ES Cell Genomes with Recombinase Systems
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von Melchner, Harald, primary and Stewart, A. Francis, additional
- Published
- 2004
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7. Contributors
- Author
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Addis, Russell C., primary, Alberts, Bruce, additional, Amit, Michal, additional, Andrews, Peter W., additional, Aoki, Hitomi, additional, Asashima, Makoto, additional, Axelman, Joyce, additional, Becker, Daniel, additional, Benvenisty, Nissim, additional, Bhatia, Mickie, additional, Blackburn, C. Clare, additional, Boiani, Michele, additional, Bonner-Weir, Susan, additional, Bowles, Josephine, additional, Boyd, Richard L., additional, Bronner-Fraser, Marianne, additional, Brunskill, Eric W., additional, Bultman, Scott, additional, Campbell, Frederick Charles, additional, Camus, Anne, additional, Carpenter, Melissa K., additional, Cavaleri, Fatima, additional, Cepko, Constance, additional, Chen, Yijing, additional, de Sousa Lopes, Susana M. Chuva, additional, Clark, Gregory O., additional, Collignon, Jérôme, additional, Collodi, Paul, additional, Cowan, Chad, additional, Daley, George Q., additional, Dani, Christian, additional, Dowell, Joshua D., additional, Draper, Jonathan S., additional, Dressler, Gregory R., additional, Drukker, Micha, additional, Durcova-Hills, Gabriela, additional, Edwards, Robert G., additional, Eisenberg, Rebecca S., additional, Elluru, Ravindhra, additional, Evans, Sir Martin, additional, Fan, Lianchun, additional, Farley, Margaret A., additional, Fekete, Donna M., additional, Field, Loren J., additional, Fink, Donald W., additional, Forrester, Lesley M., additional, Fuller, Margaret T., additional, Furue, Miho, additional, Garbers, David L., additional, Gardner, Richard L., additional, Gearhart, John D., additional, Gerecht-Nir, Sharon, additional, Gill, Jason W., additional, Gonzalez, Rodolfo, additional, Gray, Daniel H.D., additional, Green, Ronald M., additional, Gropp, Michal, additional, Haagensen, Alexandra, additional, Hamra, F. Kent, additional, Harvey, Richard P., additional, Hawes, Susan M., additional, Hayashi, Shin-Ichi, additional, Hazlehurst, Anne L., additional, Hemmi, Hiroaki, additional, Hisatsune, Hiroshi, additional, Huettner, James, additional, Huntsman, Bradley, additional, Iéhlé, Catherine, additional, Imitola, Jamie, additional, Itskovitz-Eldor, Joseph, additional, Jaenisch, Rudolf, additional, Johnson, Penny A., additional, Jones, D. Leanne, additional, Jones, Elizabeth A., additional, Karsenty, Gerard, additional, Katz, Gil, additional, Kaur, Pritinder, additional, Kelly, Robert G., additional, Kent, Kathleen C., additional, Kerr, Candace L., additional, Khademhosseini, Ali, additional, Khaner, Hanita, additional, Kintner, Chris, additional, Klimanskaya, Irina, additional, Kondoh, Nobuyuki, additional, Koopman, Peter, additional, Koyano-Nakagawa, Naoko, additional, Kraszewski, Jennifer N., additional, Krumlauf, Robb, additional, Kunath, Tilo, additional, Kunisada, Takahiro, additional, Langer, Robert, additional, Lanza, Robert, additional, Lee, Jean Pyo, additional, Levenberg, Shulamit, additional, Levine, S. Robert, additional, Lin, Haifan, additional, Littlefield, John W., additional, Lysaght, Michael J., additional, Mack, Fiona A., additional, Magnuson, Terry, additional, Malashicheva, Anna, additional, Mandelboim, Ofer, additional, Manley, Nancy R., additional, Matthaei, Klaus I., additional, Mayshar, Yoav, additional, McDonald, John W., additional, McLaren, Dame Anne, additional, McMahon, Jill, additional, Meissner, Alexander, additional, von Melchner, Harald, additional, Melton, Douglas A., additional, Montgomery, Nathan, additional, Moore, Mary Tyler, additional, Motohashi, Tsutomu, additional, Mueller, Franz-Josef, additional, Mummery, Christine, additional, Nishikawa, Satomi, additional, Nishikawa, Shin-Ichi, additional, Nagy, Andras, additional, Niwa, Hitoshi, additional, Okuyama, Hiromi, additional, Ourednik, Jitka, additional, Ourednik, Vaclav, additional, Oyamada, Masahito, additional, Oyamada, Yumiko, additional, Papaioannou, Virginia E., additional, Park, Kook I., additional, Patterson, Ethan S., additional, Patterson, Larry T., additional, Pébay, Alice, additional, Pera, Martin F., additional, Perea-Gomez, Aitana, additional, Perry, Anthony C.F., additional, Petitte, James N., additional, Phillips, Blaine W., additional, Potter, S. Steven, additional, Rai, Arti K., additional, Reeve, Christopher, additional, Reubinoff, Benjamin, additional, Rossant, Janet, additional, Rubart, Michael, additional, Savatier, Pierre, additional, Schöler, Hans, additional, Schulz, Cordula, additional, Schultz, Nikolaus, additional, Shamblott, Michael J., additional, Sidman, Richard L., additional, Simon, M. Celeste, additional, Snyder, Evan Y., additional, Stewart, A. Francis, additional, Studer, Lorenz, additional, Surani, Azim, additional, Takamatsu, Tetsuro, additional, Teng, Yang D., additional, Thesleff, Irma, additional, Thomson, James A., additional, Tosh, David, additional, Trainor, Paul, additional, Trounson, Alan O., additional, Tsuneto, Motokazu, additional, Tummers, Mark, additional, Upjohn, Edward, additional, Varigos, George, additional, Vernochet, Cécile, additional, Vivian, Jay L., additional, Wang, Zhongde, additional, Weir, Gordon C., additional, Wert, Susan E., additional, Whitsett, Jeffrey A., additional, Wininger, J. David, additional, Wu, Zhuoru, additional, Xu, Chunhui, additional, Yamane, Toshiyuki, additional, Yamashita, Jun, additional, Yamashita, Yukiko M., additional, Yamazaki, Hidetoshi, additional, Zoloth, Laurie, additional, Zwaka, Thomas P., additional, and Zweigerdt, Robert, additional
- Published
- 2004
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8. Analyzing Hormone Regulation of Transcription by Genomic Footprinting
- Author
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Reik, Andreas, primary, Schütz, Günther, additional, and Stewart, A. Francis, additional
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- 1997
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9. Hormonal and liver-specific control of expression of the tyrosine aminotransferase gene
- Author
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NITSCH, DORIS, primary, RUPPERT, SIEGFRIED, additional, KELSEY, GAVIN, additional, SCHEDL, ANDREAS, additional, WEIH, FALK, additional, STEWART, A. FRANCIS, additional, STRÄHLE, UWE, additional, SCHMID, WOLFGANG, additional, DE VACK, CAROL, additional, REIK, ANDREAS, additional, BOSHART, MICHAEL, additional, and SCHÜTZ, GÜNTHER, additional
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- 1991
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10. Expressing cytotoxic compounds in Escherichia coli Nissle 1917 for tumor-targeting therapy.
- Author
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Li R, Helbig L, Fu J, Bian X, Herrmann J, Baumann M, Stewart AF, Müller R, Li A, Zips D, and Zhang Y
- Subjects
- Animals, Cell Line, Tumor, Female, Humans, Mice, Mice, Nude, Multigene Family, Peptides administration & dosage, Peptides, Cyclic administration & dosage, Polyketides administration & dosage, Probiotics, Recombinant Proteins administration & dosage, Drug Delivery Systems, Escherichia coli genetics, Escherichia coli Proteins pharmacology, Genetic Engineering methods, Neoplasms therapy
- Abstract
Abnormal blood vessels and hypoxic and necrotic regions are common features of solid tumors and related to the malignant phenotype and therapy resistance. Certain obligate or facultative anaerobic bacteria exhibit inherent ability to colonize and proliferate within solid tumors in vivo. Escherichia coli Nissle 1917 (EcN), a non-pathogenic probiotic in European markets, has been known to proliferate selectively in the interface between the viable and necrotic regions of solid tumors. The objective of this study was to establish a tumor-targeting therapy system using the genetically engineered EcN for targeted delivery of cytotoxic compounds, including colibactin, glidobactin and luminmide. Biosynthetic gene clusters of these cytotoxic compounds were introduced into EcN and the corresponding compounds were detected in the resultant recombinant EcN strains. The recombinant EcN showed significant cytotoxic activity in vitro and in vivo as well, and significantly suppressed the tumor growth. Together, this study confirmed efficient tumor-targeting colonization of EcN and demonstrated its potentiality in the tumor-specific delivery of cytotoxic compounds as a new tumor-targeting therapy system., (Copyright © 2018. Published by Elsevier Masson SAS.)
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- 2019
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11. SETD1A protects HSCs from activation-induced functional decline in vivo.
- Author
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Arndt K, Kranz A, Fohgrub J, Jolly A, Bledau AS, Di Virgilio M, Lesche M, Dahl A, Höfer T, Stewart AF, and Waskow C
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- Animals, Histone-Lysine N-Methyltransferase genetics, Mice, Mice, Knockout, Myeloid-Lymphoid Leukemia Protein genetics, Myeloid-Lymphoid Leukemia Protein metabolism, Cell Proliferation, DNA Damage, DNA Repair, Hematopoietic Stem Cells enzymology, Histone-Lysine N-Methyltransferase metabolism
- Abstract
The regenerative capacity of hematopoietic stem cells (HSCs) is limited by the accumulation of DNA damage. Conditional mutagenesis of the histone 3 lysine 4 (H3K4) methyltransferase, Setd1a , revealed that it is required for the expression of DNA damage recognition and repair pathways in HSCs. Specific deletion of Setd1a in adult long-term (LT) HSCs is compatible with adult life and has little effect on the maintenance of phenotypic LT-HSCs in the bone marrow. However, SETD1A-deficient LT-HSCs lose their transcriptional cellular identity, accompanied by loss of their proliferative capacity and stem cell function under replicative stress in situ and after transplantation. In response to inflammatory stimulation, SETD1A protects HSCs and progenitors from activation-induced attrition in vivo. The comprehensive regulation of DNA damage responses by SETD1A in HSCs is clearly distinct from the key roles played by other epigenetic regulators, including the major leukemogenic H3K4 methyltransferase MLL1, or MLL5, indicating that HSC identity and function is supported by cooperative specificities within an epigenetic framework., (© 2018 by The American Society of Hematology.)
- Published
- 2018
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12. HIF prolyl hydroxylase 2 (PHD2) is a critical regulator of hematopoietic stem cell maintenance during steady-state and stress.
- Author
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Singh RP, Franke K, Kalucka J, Mamlouk S, Muschter A, Gembarska A, Grinenko T, Willam C, Naumann R, Anastassiadis K, Stewart AF, Bornstein S, Chavakis T, Breier G, Waskow C, and Wielockx B
- Subjects
- Animals, Bone Marrow Transplantation, Cell Cycle, Cell Differentiation, Hematopoietic Stem Cells metabolism, Hypoxia-Inducible Factor 1, alpha Subunit, Hypoxia-Inducible Factor-Proline Dioxygenases, Integrases metabolism, Mice, Mice, Inbred C57BL, Mice, Knockout, Multipotent Stem Cells metabolism, Smad7 Protein metabolism, Hematopoietic Stem Cells cytology, Hypoxia physiopathology, Multipotent Stem Cells cytology, Procollagen-Proline Dioxygenase physiology, Stress, Physiological
- Abstract
Hypoxia is a prominent feature in the maintenance of hematopoietic stem cell (HSC) quiescence and multipotency. Hypoxia-inducible factor (HIF) prolyl hydroxylase domain proteins (PHDs) serve as oxygen sensors and may therefore regulate this system. Here, we describe a mouse line with conditional loss of HIF prolyl hydroxylase 2 (PHD2) in very early hematopoietic precursors that results in self-renewal of multipotent progenitors under steady-state conditions in a HIF1α- and SMAD7-dependent manner. Competitive bone marrow (BM) transplantations show decreased peripheral and central chimerism of PHD2-deficient cells but not of the most primitive progenitors. Conversely, in whole BM transfer, PHD2-deficient HSCs replenish the entire hematopoietic system and display an enhanced self-renewal capacity reliant on HIF1α. Taken together, our results demonstrate that loss of PHD2 controls the maintenance of the HSC compartment under physiological conditions and causes the outcompetition of PHD2-deficient hematopoietic cells by their wild-type counterparts during stress while promoting the self-renewal of very early hematopoietic progenitors.
- Published
- 2013
- Full Text
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13. The histone demethylase UTX regulates stem cell migration and hematopoiesis.
- Author
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Thieme S, Gyárfás T, Richter C, Özhan G, Fu J, Alexopoulou D, Muders MH, Michalk I, Jakob C, Dahl A, Klink B, Bandola J, Bachmann M, Schröck E, Buchholz F, Stewart AF, Weidinger G, Anastassiadis K, and Brenner S
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- Animals, Cells, Cultured, Embryo, Nonmammalian, Female, Gene Expression Regulation, Developmental physiology, Gene Expression Regulation, Enzymologic physiology, HEK293 Cells, Hematopoietic Stem Cells metabolism, Histone Demethylases genetics, Histone Demethylases metabolism, Humans, Male, Mice, Mice, Inbred C57BL, Mice, Knockout, Zebrafish embryology, Zebrafish genetics, Cell Movement genetics, Hematopoiesis genetics, Hematopoietic Stem Cells physiology, Histone Demethylases physiology
- Abstract
Regulated migration of hematopoietic stem cells is fundamental for hematopoiesis. The molecular mechanisms underlying stem cell trafficking are poorly defined. Based on a short hairpin RNA library and stromal cell-derived factor-1 (SDF-1) migration screening assay, we identified the histone 3 lysine 27 demethylase UTX (Kdm6a) as a novel regulator for hematopoietic cell migration. Using hematopoietic stem and progenitor cells from our conditional UTX knockout (KO) mice, we were able to confirm the regulatory function of UTX on cell migration. Moreover, adult female conditional UTX KO mice displayed myelodysplasia and splenic erythropoiesis, whereas UTX KO males showed no phenotype. During development, all UTX KO female and a portion of UTX KO male embryos developed a cardiac defect, cranioschisis, and died in utero. Therefore, UTY, the male homolog of UTX, can compensate for UTX in adults and partially during development. Additionally, we found that UTX knockdown in zebrafish significantly impairs SDF-1/CXCR4-dependent migration of primordial germ cells. Our data suggest that UTX is a critical regulator for stem cell migration and hematopoiesis.
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- 2013
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14. Conformational adaptability of Redbeta during DNA annealing and implications for its structural relationship with Rad52.
- Author
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Erler A, Wegmann S, Elie-Caille C, Bradshaw CR, Maresca M, Seidel R, Habermann B, Muller DJ, and Stewart AF
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- Base Pairing, Binding Sites, DNA, Single-Stranded ultrastructure, Microscopy, Atomic Force, Protein Structure, Quaternary, Rad52 DNA Repair and Recombination Protein metabolism, Rad52 DNA Repair and Recombination Protein ultrastructure, Recombination, Genetic, DNA, Single-Stranded chemistry, Rad52 DNA Repair and Recombination Protein chemistry
- Abstract
Single-strand annealing proteins, such as Redbeta from lambda phage or eukaryotic Rad52, play roles in homologous recombination. Here, we use atomic force microscopy to examine Redbeta quaternary structure and Redbeta-DNA complexes. In the absence of DNA, Redbeta forms a shallow right-handed helix. The presence of single-stranded DNA (ssDNA) disrupts this structure. Upon addition of a second complementary ssDNA, annealing generates a left-handed helix that incorporates 14 Redbeta monomers per helical turn, with each Redbeta monomer annealing approximately 11 bp of DNA. The smallest stable annealing intermediate requires 20 bp DNA and two Redbeta monomers. Hence, we propose that Redbeta promotes base pairing by first increasing the number of transient interactions between ssDNAs. Then, annealing is promoted by the binding of a second Redbeta monomer, which nucleates the formation of a stable annealing intermediate. Using threading, we identify sequence similarities between the RecT/Redbeta and the Rad52 families, which strengthens previous suggestions, based on similarities of their quaternary structures, that they share a common mode of action. Hence, our findings have implications for a common mechanism of DNA annealing mediated by single-strand annealing proteins including Rad52.
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- 2009
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15. Metabolic engineering of Pseudomonas putida for methylmalonyl-CoA biosynthesis to enable complex heterologous secondary metabolite formation.
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Gross F, Ring MW, Perlova O, Fu J, Schneider S, Gerth K, Kuhlmann S, Stewart AF, Zhang Y, and Müller R
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- Acyl Coenzyme A biosynthesis, Amino Acid Sequence, Gene Expression Regulation, Gene Transfer Techniques, Methacrylates metabolism, Molecular Sequence Data, Myxococcales genetics, Operon genetics, Sequence Alignment, Thiazoles metabolism, Acyl Coenzyme A genetics, Acyl Coenzyme A metabolism, Genetic Engineering methods, Pseudomonas putida genetics, Pseudomonas putida metabolism
- Abstract
An operon consisting of three open reading frames, annotated in silico as methylmalonyl-CoA (mm-CoA) epimerase, mm-CoA mutase (MCM), and meaB, was identified in the sequencing project of the myxobacterium Sorangium cellulosum So ce56. This putative MCM pathway operon was subcloned from a bacterial artificial chromosome by Red/ET recombineering onto a minimal replicon derived from p15A. This plasmid was modified for integration and heterologous expression in Pseudomonas putida to enable the production of complex secondary metabolites requiring mm-CoA as precursor. Methylmalonate was identified in the recombinant P. putida strain by an analysis method based on gas chromatography/mass spectrometry. The engineered strain is able to synthesize polyketides requiring mm-CoA as an extender unit, which was demonstrated by the production of myxothiazol after integration of the biosynthetic gene cluster into the chromosome, followed by induction of expression.
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- 2006
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16. Uncoupling of unwinding from DNA synthesis implies regulation of MCM helicase by Tof1/Mrc1/Csm3 checkpoint complex.
- Author
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Nedelcheva MN, Roguev A, Dolapchiev LB, Shevchenko A, Taskov HB, Shevchenko A, Stewart AF, and Stoynov SS
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- Cell Cycle physiology, DNA Polymerase I metabolism, DNA-Binding Proteins, Hydroxyurea metabolism, Macromolecular Substances, Nucleic Acid Conformation, Plasmids genetics, Plasmids metabolism, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae metabolism, Cell Cycle Proteins metabolism, DNA Helicases metabolism, DNA Replication, DNA, Superhelical biosynthesis, DNA, Superhelical chemistry, DNA, Superhelical metabolism, Saccharomyces cerevisiae Proteins metabolism
- Abstract
The replicative DNA helicases can unwind DNA in the absence of polymerase activity in vitro. In contrast, replicative unwinding is coupled with DNA synthesis in vivo. The temperature-sensitive yeast polymerase alpha/primase mutants cdc17-1, pri2-1 and pri1-m4, which fail to execute the early step of DNA replication, have been used to investigate the interaction between replicative unwinding and DNA synthesis in vivo. We report that some of the plasmid molecules in these mutant strains became extensively negatively supercoiled when DNA synthesis is prevented. In contrast, additional negative supercoiling was not detected during formation of DNA initiation complex or hydroxyurea replication fork arrest. Together, these results indicate that the extensive negative supercoiling of DNA is a result of replicative unwinding, which is not followed by DNA synthesis. The limited number of unwound plasmid molecules and synthetic lethality of polymerase alpha or primase with checkpoint mutants suggest a checkpoint regulation of the replicative unwinding. In concordance with this suggestion, we found that the Tof1/Csm3/Mrc1 checkpoint complex interacts directly with the MCM helicase during both replication fork progression and when the replication fork is stalled.
- Published
- 2005
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17. Heterologous expression of a myxobacterial natural products assembly line in pseudomonads via red/ET recombineering.
- Author
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Wenzel SC, Gross F, Zhang Y, Fu J, Stewart AF, and Müller R
- Subjects
- DNA, Recombinant genetics, Gene Transfer Techniques, Genes, Bacterial genetics, Multigene Family physiology, Myxococcales genetics, Pseudomonas genetics, Species Specificity, Red Fluorescent Protein, DNA, Recombinant biosynthesis, Escherichia coli genetics, Genetic Engineering methods, Luminescent Proteins biosynthesis, Luminescent Proteins genetics, Myxococcales metabolism, Protein Processing, Post-Translational genetics, Pseudomonas metabolism
- Abstract
Natural products of microbial origin are widely used as pharmaceuticals and in agrochemistry. These compounds are often biosynthesized by multifunctional megasynthetases whose genetic engineering and heterologous expression offer considerable promise, especially if the natural hosts are genetically difficult to handle, slow growing, unculturable, or even unknown. We describe a straightforward strategy that combines the power of advanced DNA engineering (recombiogenic cloning) in Escherichia coli with the utility of pseudomonads as the heterologous host for the analysis and mutagenesis of known and unknown secondary metabolite pathways. The myxochromide S biosynthetic gene cluster from Stigmatella aurantiaca was rebuilt and engineered in E. coli to contain the elements required for expression in pseudomonads. The successful production in Pseudomonas putida, at unprecedented levels, demonstrates the feasibility of the new approach to the analysis and mutagenesis of these important pathways.
- Published
- 2005
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18. Stepwise manipulation of DNA specificity in Flp recombinase: progressively adapting Flp to individual and combinatorial mutations in its target site.
- Author
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Voziyanov Y, Konieczka JH, Stewart AF, and Jayaram M
- Subjects
- Base Pairing, Base Sequence, Catalysis, DNA chemistry, DNA Nucleotidyltransferases chemistry, Genes, Reporter genetics, Lysine genetics, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Engineering, Saccharomyces cerevisiae enzymology, Saccharomyces cerevisiae genetics, Structure-Activity Relationship, Substrate Specificity, DNA genetics, DNA metabolism, DNA Nucleotidyltransferases genetics, DNA Nucleotidyltransferases metabolism, Directed Molecular Evolution, Mutation genetics, Recombination, Genetic
- Abstract
The Flp protein from Saccharomyces cerevisiae is one of the site-specific tyrosine family recombinases that are used widely in genomic engineering. As a first step towards mediating directed DNA rearrangements at non-native Flp recombination targets (mFRTs), we have evolved three separate groups of Flp variants that preferentially act on mFRTs containing substitutions at the first, seventh or both positions of the Flp-binding elements. The variants that recombine the double-mutant mFRT contain a subset of the mutations present in those that are active on the single-mutant mFRTs, plus additional mutations. Specificity for and discrimination between target sites, effected primarily by amino acid residues that contact DNA, can be modulated by those that do not interact with DNA or with a DNA-contacting residue. The degree of modulation can range from relaxed DNA specificity to almost completely altered specificity. Our results suggest that combined DNA shuffling and mutagenesis of libraries of Flp variants active on distinct mFRTs can yield variants that can recombine mFRTs containing combinations of the individual mutations.
- Published
- 2003
- Full Text
- View/download PDF
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