HdeB chaperone activity is coupled to its intrinsic dynamic properties

doi:10.1038/srep16856

CORC > 北京大学 > 化学与分子工程学院

	HdeB chaperone activity is coupled to its intrinsic dynamic properties
	Ding, Jienv ; Yang, Chengfeng ; Niu, Xiaogang ; Hu, Yunfei ; Jin, Changwen
刊名	SCIENTIFIC REPORTS
	2015
关键词	MODEL-FREE APPROACH MAGNETIC-RESONANCE RELAXATION TORSION ANGLE DYNAMICS ACID RESISTANCE ENTERIC BACTERIA PERIPLASMIC PROTEIN CHEMICAL-EXCHANGE SUBSTRATE-BINDING NOE ASSIGNMENT NMR
DOI	10.1038/srep16856
英文摘要	Enteric bacteria encounter extreme acidity when passing through hosts' stomach. Since the bacterial periplasmic space quickly equilibrates with outer environment, an efficient acid resistance mechanism is essential in preventing irreversible protein denaturation/aggregation and maintaining bacteria viability. HdeB, along with its homolog HdeA, was identified as a periplasmic acid-resistant chaperone. Both proteins exist as homodimers and share similar monomeric structures under neutral pH, while showing different dimeric packing interfaces. Previous investigations show that HdeA functions through an acid-induced dimer-to-monomer transition and partial unfolding at low pH (pH 2-3), resulting in exposure of hydrophobic surfaces that bind substrate proteins. In contrast, HdeB appears to have a much higher optimal activation pH (pH 4-5), under which condition the protein maintains a well-folded dimer and the mechanism for its chaperone activity remains elusive. Herein, we present an NMR study of HdeB to investigate its dynamic properties. Our results reveal that HdeB undergoes significant micro- to milli-second timescale conformational exchanges at neutral to near-neutral pH, under the later condition it exhibits optimal activity. The current study indicates that HdeB activation is coupled to its intrinsic dynamics instead of structural changes, and therefore its functional mechanism is apparently different from HdeA.; National Natural Science Foundation of China [31370718]; SCI(E); PubMed; ARTICLE; yunfei@pku.edu.cn; changwen@pku.edu.cn; 16856; 5
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/416598]
专题	化学与分子工程学院生命科学学院
推荐引用方式 GB/T 7714	Ding, Jienv,Yang, Chengfeng,Niu, Xiaogang,et al. HdeB chaperone activity is coupled to its intrinsic dynamic properties[J]. SCIENTIFIC REPORTS,2015.
APA	Ding, Jienv,Yang, Chengfeng,Niu, Xiaogang,Hu, Yunfei,&Jin, Changwen.(2015).HdeB chaperone activity is coupled to its intrinsic dynamic properties.SCIENTIFIC REPORTS.
MLA	Ding, Jienv,et al."HdeB chaperone activity is coupled to its intrinsic dynamic properties".SCIENTIFIC REPORTS (2015).