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Modular structure of the trigger factor required for high activity in protein folding.

Abstract：

:The Escherichia coli trigger factor is a peptidyl-prolyl cis/trans isomerase (PPIase) which catalyzes proline-limited protein folding extremely well. It has been found associated with nascent protein chains as well as with the chaperone GroEL. The trigger factor utilizes protein regions outside the central catalytic domain for catalyzing refolding of unfolded proteins efficiently. Here we produced several fragments which encompass individual domains or combinations of the middle FKBP-like domain (M) with the N-terminal (N) and C-terminal (C) regions, respectively. These fragments appear to be stably folded. They show ordered structure and cooperative urea-induced unfolding transitions, and the far-UV CD spectrum of the intact trigger factor is well represented by the sum of the spectra of the fragments. This suggests that the native trigger factor shows a modular structure, which is composed of three fairly independent folding units. In the intact protein there is a slight mutual stabilization of these units. The high enzymatic activity in protein folding could not be restored by fusing alternatively the N or the C-terminal regions to the catalytic domain (in NM and MC constructs, respectively). Surprisingly, the high folding activity of the intact trigger factor has been regained partially by functional complementation of the overlapping NM and MC constructs.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Zarnt T,Tradler T,Stoller G,Scholz C,Schmid FX,Fischer G

doi

10.1006/jmbi.1997.1206

subject

Has Abstract

pub_date

1997-09-05 00:00:00

pages

827-37

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(97)91206-7

journal_volume

271

pub_type

杂志文章

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