Abstract:
:Biogenesis in prokaryotes and eukaryotes requires the insertion of α-helical proteins into cellular membranes for which they use universally conserved cellular machineries. In bacterial inner membranes, insertion is facilitated by YidC insertase and SecYEG translocon working individually or cooperatively. How insertase and translocon fold a polypeptide into the native protein in the membrane is largely unknown. We apply single-molecule force spectroscopy assays to investigate the insertion and folding process of single lactose permease (LacY) precursors assisted by YidC and SecYEG. Both YidC and SecYEG initiate folding of the completely unfolded polypeptide by inserting a single structural segment. YidC then inserts the remaining segments in random order, whereas SecYEG inserts them sequentially. Each type of insertion process proceeds until LacY folding is complete. When YidC and SecYEG cooperate, the folding pathway of the membrane protein is dominated by the translocase. We propose that both of the fundamentally different pathways along which YidC and SecYEG insert and fold a polypeptide are essential components of membrane protein biogenesis.
journal_name
Sci Advjournal_title
Science advancesauthors
Serdiuk T,Steudle A,Mari SA,Manioglu S,Kaback HR,Kuhn A,Müller DJdoi
10.1126/sciadv.aau6824subject
Has Abstractpub_date
2019-01-30 00:00:00pages
eaau6824issue
1issn
2375-2548pii
aau6824journal_volume
5pub_type
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