Literature DB >> 19557328

Posttranslational modulation on the biological activities of molecular chaperones.

ZengYi CHANG1.   

Abstract

Molecular chaperones are a family of proteins that were first noticed to exist about 45 years ago from their increased transcription under heat shock conditions. As a result, the regulation of their encoding genes has been subject to extensive studies. Recent studies revealed that the biological activities of molecular chaperones can also be effectively modulated at the protein level. The ways of modulation so far elucidated include allosteric effect, covalent modification, protein-protein interaction, and conformational alteration induced by such macro-environmental conditions as temperature and pH. These latter aspects were reviewed here. Emphasized here is the importance of such immediate structural alterations that lead to an immediate activity increase, providing the immediate protection needed for the cells to survive the stress conditions.

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Year:  2009        PMID: 19557328     DOI: 10.1007/s11427-009-0084-6

Source DB:  PubMed          Journal:  Sci China C Life Sci        ISSN: 1006-9305


  2 in total

1.  Functional interaction of heat shock protein 90 and Beclin 1 modulates Toll-like receptor-mediated autophagy.

Authors:  Congfeng Xu; Jin Liu; Li-Chung Hsu; Yunping Luo; Rong Xiang; Tsung-Hsien Chuang
Journal:  FASEB J       Date:  2011-05-04       Impact factor: 5.191

2.  Transcriptome response to temperature stress in the wolf spider Pardosa pseudoannulata (Araneae: Lycosidae).

Authors:  Rong Xiao; Liang Wang; Yingshuai Cao; Guren Zhang
Journal:  Ecol Evol       Date:  2016-04-20       Impact factor: 2.912

  2 in total

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