Abstract:
:The Sec61 translocon mediates the translocation of proteins across the endoplasmic reticulum membrane and the lateral integration of transmembrane segments into the lipid bilayer. The structure of the idle translocon is closed by a lumenal plug domain and a hydrophobic constriction ring. To test the function of the apolar constriction, we have mutated all six ring residues of yeast Sec61p to more hydrophilic, bulky, or even charged amino acids (alanines, glycines, serines, tryptophans, lysines, or aspartates). The translocon was found to be surprisingly tolerant even to the charge mutations in the constriction ring, because growth and translocation efficiency were not drastically affected. Most interestingly, ring mutants were found to affect the integration of hydrophobic sequences into the lipid bilayer, indicating that the translocon does not simply catalyze the partitioning of potential transmembrane segments between an aqueous environment and the lipid bilayer but that it also plays an active role in setting the hydrophobicity threshold for membrane integration.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Junne T,Kocik L,Spiess Mdoi
10.1091/mbc.e10-01-0060subject
Has Abstractpub_date
2010-05-15 00:00:00pages
1662-70issue
10eissn
1059-1524issn
1939-4586pii
E10-01-0060journal_volume
21pub_type
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