Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroEL.

Abstract:

:The GroE chaperonin system facilitates protein folding in an ATP-dependent manner. It has remained unclear why some proteins are obligate clients of the GroE system, whereas other closely related proteins are able to fold efficiently in its absence. Factors that cause folding to be slower affect kinetic partitioning between spontaneous folding and chaperone binding in favor of the latter. One such potential factor is contact order (CO), which is the average separation in sequence between residues that are in contact in the native structure. Here, we generated variants of enhanced green fluorescent protein with different COs using circular permutations. We found that GroE dependence in vitro and in vivo increases with increasing CO. Thus, our results show that CO is relevant not only for folding in vitro of relatively simple model systems but also for chaperonin dependence and folding in vivo.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Bandyopadhyay B,Mondal T,Unger R,Horovitz A

doi

10.1016/j.bpj.2018.11.019

subject

Has Abstract

pub_date

2019-01-08 00:00:00

pages

42-48

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(18)31284-0

journal_volume

116

pub_type

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