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 Jjournal_title
Biophysical journalauthors
Bandyopadhyay B,Mondal T,Unger R,Horovitz Adoi
10.1016/j.bpj.2018.11.019subject
Has Abstractpub_date
2019-01-08 00:00:00pages
42-48issue
1eissn
0006-3495issn
1542-0086pii
S0006-3495(18)31284-0journal_volume
116pub_type
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