多肽诱导的大肠杆菌DegP(HtrA)蛋白酶的构象变化

doi:10.3321/j.issn:1000-3282.2006.02.012

CORC > 北京大学 > 生命科学学院

	多肽诱导的大肠杆菌DegP(HtrA)蛋白酶的构象变化; Peptide Induced Conformational Changes of E. Coli DegP (HtrA) Protease
	张雪峰 ; 郑益新 ; 昌增益
刊名	生物化学与生物物理进展
	2006
关键词	DegP 构象变化多肽机制 DegP conformational change peptide mechanism DegP conformational change peptide mechanism
DOI	10.3321/j.issn:1000-3282.2006.02.012
英文摘要	具有分子伴侣和蛋白酶双重活性的大肠杆菌DegP蛋白,在热休克和其他应激条件下,对于降解和清除膜间质中变性或损伤的蛋白质起着十分重要的作用.到目前为止,已有几种蛋白质被鉴定出是DegP的天然底物.以前的研究表明,DegP的体内底物之一,PapG菌毛蛋白的羧基端多肽能够激活DegP的蛋白酶活性.然而这种激活的机制及生理意义均未见报道.用合成的PapG菌毛蛋白的羧基端多肽对这种激活的机制进行了初步研究.结果表明,DegP与多肽结合后发生了可检测的构象变化.圆二色性光谱结果显示,结合多肽后DegP的二级结构和三级结构均发生了一定的变化.凝胶排阻层析和动态光散射实验也揭示出DegP分子在一定程度上变小.进一步实验表明,DegP在多肽存在下,其疏水表面和催化位点均有所暴露.荧光各向异性结果显示出DegP在结合多肽后其构象柔性降低.对上述结果的意义进行了探讨.; The DegP protein, functioning as both chaperone and protease, plays a critical role in degrading and removing denatured or damaged proteins in the cellular envelope during heat shock and other stresses. So far, several proteins have been identified as its natural targets. A carboxyle-terminal peptide derived from the PapG pilus, one of the in vivo substrates for DegP, has been shown to activate the protease. Nevertheless, neither the details nor the physiological implications of such activation have been studied. The evidence that DegP undergoes conformational changes upon binding the peptide derived from C-terminal sequence of pilus subunit PapG has been presented. It demonstrated that upon binding this peptide, detectable changes can be observed for both secondary and tertiary structures of DegP, as examined by CD spectroscopy. Gel filtration and dynamic light scattering analysis also revealed that the size of DegP becomes smaller to a minor extent. Moreover, both the hydrophobic surfaces and catalytic sites of DegP were found to expose slightly in the presence of the peptide. Upon peptide binding, a less flexible and more rigid conformation of DegP was obtained as analyzed by fluorescence anisotropy. The physiological implications of these observations for DegP are discussed.; 国家重点基础研究发展计划(973计划); 中国科学院资助项目; SCI(E); 中文核心期刊要目总览(PKU); 中国科技核心期刊(ISTIC); 0; 2; 183-189; 33
语种	中文
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/252351]
专题	生命科学学院
推荐引用方式 GB/T 7714	张雪峰,郑益新,昌增益. 多肽诱导的大肠杆菌DegP(HtrA)蛋白酶的构象变化, Peptide Induced Conformational Changes of E. Coli DegP (HtrA) Protease[J]. 生物化学与生物物理进展,2006.
APA	张雪峰,郑益新,&昌增益.(2006).多肽诱导的大肠杆菌DegP(HtrA)蛋白酶的构象变化.生物化学与生物物理进展.
MLA	张雪峰,et al."多肽诱导的大肠杆菌DegP(HtrA)蛋白酶的构象变化".生物化学与生物物理进展 (2006).