The Conformation of Substrate and Oligomeric State of DegP Regulate Its Chaperone and Protease Funct

来源 :中国化学会第三届全国生物物理化学会议暨国际华人生物物理化学发展论坛 | 被引量 : 0次 | 上传用户：wangweiche

【摘要】

：

The heat-shock protein DegP is essential for the survival of Escherichia coli cells at elevated temperatures.As a protease to degrade misfolded proteins in the

【作者】

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Zhi-Xin Lyu Xin Sheng Zhao

【机构】

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BeijingNationalLaboratoryforMolecularSciences,StateKeyLaboratoryforStructuralChemistryofUnstableandS

【出处】

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中国化学会第三届全国生物物理化学会议暨国际华人生物物理化学发展论坛

【发表日期】

：

2014年7期

【关键词】

：

Protein quality control Protease Molecular chaperone smFRET

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The heat-shock protein DegP is essential for the survival of Escherichia coli cells at elevated temperatures.As a protease to degrade misfolded proteins in the periplasm,DegP is proposed to have chaperone activity as well.However,the mechanisms regulating this dual-function are poorly understood.Here we show that OmpC can be directly transported froln Skp to DegP and DegP can not degrade such kinds of OmpC (Figure A).

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The Conformation of Substrate and Oligomeric State of DegP Regulate Its Chaperone and Protease Funct

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