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Unique structural modulation of a non-native substrate by cochaperone DnaJ.

Abstract：

:The role of bacterial DnaJ protein as a cochaperone of DnaK is strongly appreciated. Although DnaJ unaccompanied by DnaK can bind unfolded as well as native substrate proteins, its role as an individual chaperone remains elusive. In this study, we demonstrate that DnaJ binds a model non-native substrate with a low nanomolar dissociation constant and, more importantly, modulates the structure of its non-native state. The structural modulation achieved by DnaJ is different compared to that achieved by the DnaK-DnaJ complex. The nature of structural modulation exerted by DnaJ is suggestive of a unique unfolding activity on the non-native substrate by the chaperone. Furthermore, we demonstrate that the zinc binding motif along with the C-terminal substrate binding domain of DnaJ is necessary and sufficient for binding and the subsequent binding-induced structural alterations of the non-native substrate. We hypothesize that this hitherto unknown structural alteration of non-native states by DnaJ might be important for its chaperoning activity by removing kinetic traps of the folding intermediates.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Tiwari S,Kumar V,Jayaraj GG,Maiti S,Mapa K

doi

10.1021/bi301543g

subject

Has Abstract

pub_date

2013-02-12 00:00:00

pages

1011-8

issue

6

eissn

0006-2960

issn

1520-4995

journal_volume

52

pub_type

杂志文章

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