Abstract:
:Precise protein folding is essential for the survival of all cells, and protein misfolding causes a number of diseases that lack effective therapies, yet the general principles governing protein folding in the cell remain poorly understood. In vivo, folding can begin cotranslationally and protein quality control at the ribosome is essential for cellular proteostasis. We directly characterize and compare the refolding and cotranslational folding trajectories of the protein HaloTag. We introduce new techniques for both measuring folding kinetics and detecting the conformations of partially folded intermediates during translation in real time. We find that, although translation does not affect the rate-limiting step of HaloTag folding, a key aggregation-prone intermediate observed during in vitro refolding experiments is no longer detectable. This rerouting of the folding pathway increases HaloTag's folding efficiency and may serve as a general chaperone-independent mechanism of quality control by the ribosome.
journal_name
Sci Advjournal_title
Science advancesauthors
Samelson AJ,Bolin E,Costello SM,Sharma AK,O'Brien EP,Marqusee Sdoi
10.1126/sciadv.aas9098subject
Has Abstractpub_date
2018-05-30 00:00:00pages
eaas9098issue
5issn
2375-2548pii
aas9098journal_volume
4pub_type
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