Abstract:
:C-tailed membrane proteins insert into the bilayer post-translationally because the hydrophobic anchor segment leaves the ribosome at the end of translation. Nevertheless, we find here evidence that the targeting of SciP to the membrane of Escherichia coli occurs co-translationally since signal elements in the N-terminal part of the SciP protein sequence are present. Two short hydrophobic sequences were identified that targeted a green fluorescent protein-SciP fusion protein to the membrane involving the signal recognition particle. After targeting, the membrane insertion of SciP is catalyzed by YidC independent of the SecYEG translocase. However, when the C-terminal tail of SciP was extended to 21 aa residues, we found that SecYEG becomes involved and makes its membrane insertion more efficient.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Pross E,Soussoula L,Seitl I,Lupo D,Kuhn Adoi
10.1016/j.jmb.2016.09.001subject
Has Abstractpub_date
2016-10-09 00:00:00pages
4218-4227issue
20eissn
0022-2836issn
1089-8638pii
S0022-2836(16)30363-1journal_volume
428pub_type
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