Differential degradation for small heat shock proteins IbpA and IbpB is   synchronized in Escherichia coli: Implications for their functional   cooperation in substrate refolding

doi:10.1016/j.bbrc.2014.08.084

CORC > 北京大学 > 生命科学学院

	Differential degradation for small heat shock proteins IbpA and IbpB is synchronized in Escherichia coli: Implications for their functional cooperation in substrate refolding
	Shi, Xiaodong ; Yan, Linxuan ; Zhang, Hanlin ; Sun, Kai ; Chang, Zengyi ; Fu, Xinmiao
刊名	生物化学与生物物理学研究通讯
	2014
关键词	Protein degradation Molecular chaperone Small heat shock protein IbpA IbpB Substrate proteins CHAPERONE-LIKE ACTIVITY ALPHA-CRYSTALLIN MULTICHAPERONE NETWORK MOLECULAR CHAPERONES IN-VIVO DISAGGREGATION EXPRESSION AGGREGATION HSP16.3 BINDING
DOI	10.1016/j.bbrc.2014.08.084
英文摘要	Small heat shock proteins (sHSPs), as a conserved family of ATP-independent molecular chaperones, are known to bind non-native substrate proteins and facilitate the substrate refolding in cooperation with ATP-dependent chaperones (e.g., DnaK and ClpB). However, how different sHSPs function in coordination is poorly understood. Here we report that IbpA and IbpB, the two sHSPs of Escherichia coli, are coordinated by synchronizing their differential in vivo degradation. Whereas the individually expressed IbpA and IbpB are respectively degraded slowly and rapidly in cells cultured under both heat shock and normal conditions, their simultaneous expression leads to a synchronized degradation at a moderate rate. Apparently, such synchronization is linked to their hetero-oligomerization and cooperation in binding substrate proteins. In addition, truncation of the flexible N- and C-terminal tails dramatically suppresses the IbpB degradation, and somehow accelerates the IbpA degradation. In view of these in vivo data, we propose that the synchronized degradation for IbpA and IbpB are crucial for their synergistic promoting effect on DnaK/ClpB-mediated substrate refolding, conceivably via the formation of IbpA-IbpB-substrate complexes. This scenario may be common for different sHSPs that interact with each other in cells. (C) 2014 Elsevier Inc. All rights reserved.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000343023900016&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology; Biophysics; SCI(E); PubMed; 0; ARTICLE; changzy@pku.edu.cn; fuxinmiao@pku.edu.cn; 3; 402-407; 452
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/189197]
专题	生命科学学院
推荐引用方式 GB/T 7714	Shi, Xiaodong,Yan, Linxuan,Zhang, Hanlin,et al. Differential degradation for small heat shock proteins IbpA and IbpB is synchronized in Escherichia coli: Implications for their functional cooperation in substrate refolding[J]. 生物化学与生物物理学研究通讯,2014.
APA	Shi, Xiaodong,Yan, Linxuan,Zhang, Hanlin,Sun, Kai,Chang, Zengyi,&Fu, Xinmiao.(2014).Differential degradation for small heat shock proteins IbpA and IbpB is synchronized in Escherichia coli: Implications for their functional cooperation in substrate refolding.生物化学与生物物理学研究通讯.
MLA	Shi, Xiaodong,et al."Differential degradation for small heat shock proteins IbpA and IbpB is synchronized in Escherichia coli: Implications for their functional cooperation in substrate refolding".生物化学与生物物理学研究通讯 (2014).