Multilevel structural characteristics for the natural substrate proteins   of bacterial small heat shock proteins

doi:10.1002/pro.2404

CORC > 北京大学 > 生命科学学院

	Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins
	Fu, Xinmiao ; Chang, Zengyi ; Shi, Xiaodong ; Bu, Dongbo ; Wang, Chao
刊名	蛋白质科学
	2014
关键词	molecular chaperone small heat shock protein protein aggregation substrate proteins IbpB Hsp20.2 CHAPERONE ALPHA-CRYSTALLIN MOLTEN GLOBULE STATES MOLECULAR CHAPERONE ESCHERICHIA-COLI IN-VIVO 1,1&apos SECONDARY STRUCTURE DENATURED PROTEINS MISSENSE MUTATION MOTOR NEUROPATHY -BI(4-ANILINO)NAPHTHALENE-5,5&apos -DISULFONIC ACID
DOI	10.1002/pro.2404
英文摘要	Small heat shock proteins (sHSPs) are ubiquitous molecular chaperones that prevent the aggregation of various non-native proteins and play crucial roles for protein quality control in cells. It is poorly understood what natural substrate proteins, with respect to structural characteristics, are preferentially bound by sHSPs in cells. Here we compared the structural characteristics for the natural substrate proteins of Escherichia coli IbpB and Deinococcus radiodurans Hsp20.2 with the respective bacterial proteome at multiple levels, mainly by using bioinformatics analysis. Data indicate that both IbpB and Hsp20.2 preferentially bind to substrates of high molecular weight or moderate acidity. Surprisingly, their substrates contain abundant charged residues but not abundant hydrophobic residues, thus strongly indicating that ionic interactions other than hydrophobic interactions also play crucial roles for the substrate recognition and binding of sHSPs. Further, secondary structure prediction analysis indicates that the substrates of low percentage of -sheets or coils but high percentage of -helices are un-favored by both IbpB and Hsp20.2. In addition, IbpB preferentially interacts with multi-domain proteins but unfavorably with + proteins as revealed by SCOP analysis. Together, our data suggest that bacterial sHSPs, though having broad substrate spectrums, selectively bind to substrates of certain structural features. These structural characteristic elements may substantially participate in the sHSP-substrate interaction and/or increase the aggregation tendency of the substrates, thus making the substrates more preferentially bound by sHSPs.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000329939900009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology; SCI(E); PubMed; 4; ARTICLE; fuxinmiao@pku.edu.cn; 2; 229-237; 23
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/189747]
专题	生命科学学院
推荐引用方式 GB/T 7714	Fu, Xinmiao,Chang, Zengyi,Shi, Xiaodong,et al. Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins[J]. 蛋白质科学,2014.
APA	Fu, Xinmiao,Chang, Zengyi,Shi, Xiaodong,Bu, Dongbo,&Wang, Chao.(2014).Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins.蛋白质科学.
MLA	Fu, Xinmiao,et al."Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins".蛋白质科学 (2014).