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344 results on '"Soll J"'

9. Structural and guanosine triphosphate/diphosphate requirements for transit peptide recognition by the cytosolic domain of the chloroplast outer envelope receptor, Toc34

Author

Schleiff, E., Soll, J., Sveshnikova, N., Tien, R., Wright, S., Dabney-Smith, C., Subramanian, C., and Bruce, B. D.

Subjects
Biochemistry -- Research, Guanosine -- Physiological aspects, Pyrophosphates -- Physiological aspects, Peptides -- Physiological aspects, Chloroplasts -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the transmembrane protein Toc34 located in the chloroplast's outer membrane envelope. Results indicate that soluble cytosolic domain of Toc34 can function as a receptor and can import into chloroplasts in a guanosine triphosphate-dependent manner.

Published
2002

13. Session 15 Cellular transport

Author

Epel, B., Yahalom, A., Katz, A., Kotlizky, G., Cohen, L., Erlanger, M., Levi, R., Levi, N., Van Lent, J., Belyaeva, N., Nasyrova, G., Simchuk, E., Buckhout, Thomas J., Buntukova, E. K., Karimova, F. G., Klochkova, E. E., Driouich, A., Staehelin, La., Frommer, W. B., Fischer, W. N., Hirner, B., Kwart, M., Lauter, F. R., Ninnemann, O., Rentsch, D., Fuks, B., Homble, F., Getz, H. P., Klein, M., Henricson, D., Opanasenko, V. K., Bergstedt, K. -G., Gardeström, P., Samuelsson, G., Janáček, K., Nešpůrková, L., Beneš, I., Metlička, R., Sigler, K., Jordi, W., Stoopen, G. M., Karnauchov, I., Cai, D., Clausmeyer, S., Herrmann, R. G., KlOsgen, R. B., Lyalin, O. O., Ktitorova, I. N., Marichev, G. A., Skobeleva, O. V., Miklós, E., Szöke, L., Kozma, P., Haydu, Zs., Erdei, L., Moshkov, A. V., Batov, A. Y., Petrussa, E., Marci’, F., Zancani, M., Dell’antone, P., Vianello, A., Seedorf, M., Soll, J., Sokolik, A. I., Yurin, V. M., Szakiel, A., Janiszowska, W., Tokarska, M., Spiewla, E., Vicente, J. A. F., Vale, M. G. P., Weig, A., Dolle, L. -O., Franz, J., Komor, E., Zagdańska, B., and Rybka, Z.

Published
1994
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17. Protein import machineries in endosymbiotic organelles

Author

Balsera, M., Soll, J., Bölter, B., Balsera, M., Soll, J., and Bölter, B.

Abstract

Chloroplast and mitochondria, the two organelles with an accepted endosymbiotic origin, have developed multiple translocation pathways to ensure the subcellular allocation of proteins synthesized by cytosolic ribosomes, and to guarantee their assembly into functional complexes in coordination also with organellar-encoded subunits. The evolution of different protein import machineries was thus essential for the development of these two organelles within cells. A general overview of the translocation machineries in chloroplast and mitochondrial membranes involved in targeting and import of nuclearencoded proteins, with special focus on plant cells where the two organelles coexist, is expounded

Published
2018

22. Redox-regulation of protein import into chloroplasts and mitochondria: Similarities and differences

Author

Stengel, A., Benz, J. P., Soll, J., and Bölter, B.

Subjects
protein import, chloroplasts, mitochondria, redox-regulation, disulfide bridges, NADP(H), Toc, Tic, Tom, ddc:630, ddc
Abstract

Redox signals play important roles in many developmental and metabolic processes, in particular in chloroplasts and mitochondria. Furthermore, redox reactions are crucial for protein folding via the formation of inter- or intramolecular disulfide bridges. Recently, redox signals were described to be additionally involved in regulation of protein import: in mitochondria, a disulfide relay system mediates retention of cystein-rich proteins in the intermembrane space by oxidizing them. Two essential proteins, the redox-activated receptor Mia40 and the sulfhydryl oxidase Erv1 participate in this pathway. In chloroplasts, it becomes apparent that protein import is affected by redox signals on both the outer and inner envelope: at the level of the Toc complex (translocon at the outer envelope of chloroplasts), the formation/reduction of disulfide bridges between the Toc components has a strong influence on import yield. Moreover, the stromal metabolic redox state seems to be sensed by the Tic complex (translocon at the inner envelope of chloroplasts) that is able to adjust translocation efficiency of a subgroup of redox-related preproteins accordingly. This review summarizes the current knowledge of these redox-regulatory pathways and focuses on similarities and differences between chloroplasts and mitochondria.

Published
2009

25. Long-term complications of central venous catheters in children

Author

Soll, J. J., van Woensel, J. B. M., van Ommen, C. H., Bos, A. P., Amsterdam institute for Infection and Immunity, Amsterdam Reproduction & Development (AR&D), Paediatric Intensive Care, Paediatric Infectious Diseases / Rheumatology / Immunology, and Other Research

Published
2007

32. The protein translocon of the plastid envelopes

Author

Vojta, Aleksandar, primary, Alavi, Marcel, additional, Becker, Thomas, additional, K�chler, Michael, additional, H�rmann, Friederike, additional, Soll, J�rgen, additional, Thomson, Rowena, additional, and Schleiff, Enrico, additional

Published
2005
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34. Intracellular localization of VDAC proteins in plants

Author

Clausen, Cathrin, primary, Ilkavets, Iryna, additional, Thomson, Rowena, additional, Philippar, Katrin, additional, Vojta, Aleksandar, additional, M�hlmann, Torsten, additional, Neuhaus, Ekkehard, additional, Fulgosi, Hrvoje, additional, and Soll, J�rgen, additional

Published
2004
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37. Chloroplast quest: A journey from the cytosol into the chloroplast and beyond.

Author

Amara, S. G., Bamberg, E., Blaustein, M. P., Grunicke, H., Jahn, R., Lederer, W. J., Miyajima, A., Murer, H., Pfanner, N., Schultz, G., Schweiger, M., Vothknecht, Ute C., and Soll, J.

Abstract

Chloroplasts are characteristic organelles of plants and algae and the site of oxygenic photosynthesis. They are surrounded by a double membrane and possess an internal membrane system, the thylakoids, on which the photosynthetic machinery is located. They originated more than 1.2 billion years ago from an endosymbiotic event between an already photosynthetic ancestor of present day cyanobacteria and a mitochondriate host cell. During the transformation of the internalized cyanobacterium into a cell organelle most of the genetic information of the endosymbiot got lost or was transferred into the nucleus of the host. Chloroplast proteins encoded by nuclear genes are synthesized on cytoplasmic ribosomes and have to be relocated into the organelle. This is achieved by a proteinaceous import machinery in the outer and inner envelope of the chloroplasts. Proteins destined for the thylakoid membrane and the thylakoid lumen are further translocated by several different pathways into or across this membrane. The subject of this review is the quest of nuclear encoded chloroplast proteins into the organelle and to their final suborganellar location. [ABSTRACT FROM AUTHOR]

Published
2002
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39. 14-3-3 proteins:a highly conserved, widespread family of eukaryotic proteins

Author

Aitken, Alastair, Collinge, D. B., van Heusden, B. P.H., Isobe, T., Roseboom, P. H., Rosenfeld, G., Soll, J., Aitken, Alastair, Collinge, D. B., van Heusden, B. P.H., Isobe, T., Roseboom, P. H., Rosenfeld, G., and Soll, J.

Abstract

A family of proteins known as 14-3-3 is currently receiving increased attention by investigators studying a broad range of biological systems, including plants and invertebrates. The outstanding feature of this family is the extraordinarily high sequence conservation observed. Current thinking indicates that these proteins may function as regulators in signal tranduction/phosphorylation mechanisms.

Published
1992

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