Disaggregases in 4 dimensions

被引：35

作者：

Barends, Thomas R. M. ^{[1
]}

Werbeck, Nicolas D. ^{[1
]}

Reinstein, Jochen ^{[1
]}

机构：

[1] Max Planck Inst Med Res, Dept Biomol Mech, D-69120 Heidelberg, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2010年 / 20卷 / 01期

关键词：

CLPB CHAPERONE; PROTEIN DISAGGREGATION; SUBUNIT INTERACTIONS; MOLECULAR CHAPERONE; TERMINAL DOMAIN; ATPASE CYCLE; COILED-COIL; AAA; BINDING; HSP104;

D O I：

10.1016/j.sbi.2009.12.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Non-destructive dissagregation of protein aggregates is a formidable task mediated by the specialized AAA+ chaperone Hsp104/ClpB in combination with the Hsp70/DnaK chaperone system. The exact mechanism of how the hexameric Hsp104/ClpB proteins perform the task of protein disaggregation or remodeling is largely unknown. The process is ATP-dependent and tight coupling between the ATPase domains within the hexameric ring-complex could be observed. While substrate translocation through the central pore of the ring-shaped hexamer appears to be a central mechanism shared with other AAA+ proteins, a middle domain unique to Hsp104/ClpB could be involved in specific features of the Hsp/ClpB mechanism and its regulation. Recent findings underline the dynamic properties of the molecular complex and might provide a basis to understand substrate interaction, regulation of disaggregation activity, and interactions with co-chaperones.

引用

页码：46 / 53

页数：8

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