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Effect of C-terminal truncation on the molecular chaperone function and dimerization of Escherichia coli trigger factor.

Abstract：

:To examine the role of the C-terminal domain in the chaperone function of trigger factor (TF), a number of truncation mutants were constructed, namely: TF419, TF389, TF380, TF360, TF344, and TF251, in which the C-terminal 13, 43, 52, 72, 88 residues or the entire C-domain were deleted, respectively. Co-expression of mutant chicken adenylate kinase (AK) with TF and the C-terminal truncation mutants was achieved using a plasmid pBVAT that allows expression of TF and AK from a single plasmid. The results show that truncation of the C-terminus of TF has only minor effect on its ability to assist AK refolding in vivo. Further, ribosome-binding experiments indicate that C-terminal truncation mutants can still bind to the ribosome and the presence of the C-terminus may in fact lower the affinity of TF for the ribosome in vivo. This indicates that the C-domain of trigger factor may not be essential for the ribosome-associated molecular chaperone function of TF. However, the purified TF C-terminal truncation mutants had a dramatically reduced ability to assist rabbit muscle GAPDH refolding in vitro and a reduced tendency to dimerize. This shows that the structural integrity of the C-terminus contributes to both the chaperone function of TF and the stability of the dimeric form.

journal_name

Biochimie

journal_title

Biochimie

authors

Zeng LL,Yu L,Li ZY,Perrett S,Zhou JM

doi

10.1016/j.biochi.2005.11.006

keywords:

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

613-9

issue

6

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(05)00271-3

journal_volume

88

pub_type

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