Molecular chaperones in biology, medicine and protein biotechnology

作者: Gregory L Blatch , Addmore Shonhai , Keoagile W Modisakeng , Fritha Hennessy , Graeme Bradley

DOI:

关键词: Cell biologyHeat shock proteinBiotechnologyHsp70Hsp90Target proteinChemical chaperoneCo-chaperoneProtein foldingBiologyChaperone (protein)

摘要: Molecular chaperones consist of several highly conserved families of proteins, many which heat shock proteins. The primary function molecular is to facilitate the folding or refolding and therefore they play an important role in diverse cellular processes including protein synthesis, translocation, or degradation proteins after cell stress. Cells are often exposed different stressors, resulting protein misfolding aggregation. It now well established that the levels certain elevated during stress provide protection cell. focus this review on impact biology, medicine biotechnology, thus covers both fundamental applied aspects chaperone biology. Attention paid functions and applications from bacterial eukaryotic cells, focusing 90 (Hsp90), 70 (Hsp70) 40 (Hsp40) classes chaperones, respectively. role these human diseases discussed, as as parts played by produced causative agents malaria trypanosomiasis. Recent advances have seen application improving yields a particular target recombinant production. prospects for targeted use over-production critically reviewed, current research at Rhodes University also discussed.

参考文章(203)
Jianwen Jiang, Alexander B. Taylor, Kondury Prasad, Yumiko Ishikawa-Brush, P. John Hart, Eileen M. Lafer, Rui Sousa, Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface. Biochemistry. ,vol. 42, pp. 5748- 5753 ,(2003) , 10.1021/BI034270G
O.O. Odunuga, V.M. Longshaw, G.L. Blatch, Hop: more than an Hsp70/Hsp90 adaptor protein BioEssays. ,vol. 26, pp. 1058- 1068 ,(2004) , 10.1002/BIES.20107
Jason C Young, Christine Schneider, F.Ulrich Hartl, In vitro evidence that hsp90 contains two independent chaperone sites FEBS Letters. ,vol. 418, pp. 139- 143 ,(1997) , 10.1016/S0014-5793(97)01363-X
Mei-Shya Chen, Adam M Silverstein, William B Pratt, Michael Chinkers, None, The Tetratricopeptide Repeat Domain of Protein Phosphatase 5 Mediates Binding to Glucocorticoid Receptor Heterocomplexes and Acts as a Dominant Negative Mutant Journal of Biological Chemistry. ,vol. 271, pp. 32315- 32320 ,(1996) , 10.1074/JBC.271.50.32315
Michael E. Cheetham, Avrom J. Caplan, Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function Cell Stress & Chaperones. ,vol. 3, pp. 28- 36 ,(1998) , 10.1379/1466-1268(1998)003<0028:SFAEOD>2.3.CO;2
Y. Zhang, E. R. P. Zuiderweg, The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 101, pp. 10272- 10277 ,(2004) , 10.1073/PNAS.0401313101
Michele Gilbert, Joanna S Albala, Accelerating code to function: sizing up the protein production line. Current Opinion in Chemical Biology. ,vol. 6, pp. 102- 105 ,(2002) , 10.1016/S1367-5931(01)00291-5
Stefan Rüdiger, Lothar Germeroth, Jens Schneider‐Mergener, Bernd Bukau, Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries The EMBO Journal. ,vol. 16, pp. 1501- 1507 ,(1997) , 10.1093/EMBOJ/16.7.1501
S E Holstein, H Ungewickell, E Ungewickell, Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin. Journal of Cell Biology. ,vol. 135, pp. 925- 937 ,(1996) , 10.1083/JCB.135.4.925