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Cytosolic HSP90 Cochaperone. HOP and FKBP Interact with Freshly Synthesized Chloroplast Preproteins of Arabidopsis

Molecular Plant 2011年第6期4卷 1133-1145页

作者： Christine Fellerer Regina Schweiger Katharina Schongruber Jurgen Soil Serena Schwenker Department of Biology 1 Botany Ludwig-Maximilians-Universitat Munchen Grobhaderner Strasse 2-4 D-82152 Planegg-Martinsried Germany Munich Center for Integrated Protein Science CiPSM Ludwig-Maximilians-Universitut Munchen Feodor-Lynen-Strasse 25 D-81377 Munich Germany

Most chloroplast and mitochondrial proteins are synthesized in the cytosol of the plant cell and have to be imported into the organelles post-translationally. Molecular chaperone. play an important role in preventing protein aggregation of freshly translated preproteins and assist in maintaining the preproteins in an import competent state. Pre- proteins can associate with HSP70, HSP90, and 14-3-3 proteins in the cytosol. In this study, we analyzed a large set of wheat germ-translated chloroplast preproteins with respect to their chaperone.binding. Our results demonstrate that the formation of distinct 14-3-3 or HSP90 containing preprotein complexes is a common feature in post-translational protein transport in addition to preproteins that seem to interact solely with HSP70. We were able to identify a diverse and extensive class of preproteins as HSP90 substrates, thus providing a tool for the investigation of HSP90 client protein association. The analyses of chimeric HSP90 and 14-3-3 binding preproteins with exchanged transit peptides indicate an involvement of both the transit peptide and the mature part of the proteins, in HSP90 binding. We identified two partner components of the HSP90 cycle, which were present in the preprotein containing high-molecular-weight complexes, the HSP70/HSP90 organizing protein HOP, as well as the immunophilin FKBP73. The results establish chloroplast preproteins as a general class of HSP90 client proteins in plants using HOP and FKBP as novel cochaperone..

关键词： Wheat germ in vitro translation chloroplast import chaperone.

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PDI-, PPI- and chaperone.catalyzed refolding of recombinant human IL-2 and GM-CSF

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Science China Chemistry 1995年第4期38卷 429-437页

作者：徐明波孟文华马贤凯 Institute of Basic Medical Sciences Beijing 100850 China

The studies on PDI-, PP1- and chaperone.catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disalfide bonds and formation of aggregates by interchains linkage, furthermore, PDI can correct, the mismatching of disulflde bonds in IL-2 isomers. PPI can increase the rate of folding reaction while chaperone.can prevent the aggregation during the folding process. In addition, there is a synergistic effect between them.

关键词： recombinant protein folding PDI PPI chaperone.

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HSP90β participates in regulation of heat shock gene expression

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Chinese Science Bulletin 1996年第20期41卷 1730-1734页

作者：王艳林沈珝琲梅树恩刘巨洪张书岭吴宁华 State Key Laboratory of Medical Molecular Biology Chinese Academy of Medical Sciences Peking Union Medical College Beijing 100005 China

Heat shock proteins (HSP) are a group of proteins highly conserved in *** play important physiological roles, usually as molecular chaperone. in living cells, and take great parts in cell protection process against stress, and in signal transduction as ***70 and HSP90 are the major HSPs expressed in human peripheral lymphocytes upon heat shock. HSP90 consists of two copies, designated as HSP90α and HSP90β. Heat shock factors (HSF), the trans regulators, participate in the regulation of HSP gene transcription. Different from HSP70 which is dramatically induced by stress, both heat shock and cold shock, HSP90 expresses at a relatively high level physiologically and may exist as complexes with various steroid receptors or some important components in signal transduction pathway, and plays a role of specific molecular chaperone. The aim of

关键词： antisense cDNA hsp90 gene molecular chaperone.

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