{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Demirci E"],"funding":["Swiss National Science Foundation"],"pagination":["18856-61"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3839696"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["110(47)"],"pubmed_abstract":["The Sec61 translocon forms a pore to translocate polypeptide sequences across the membrane and offers a lateral gate for membrane integration of hydrophobic (H) segments. A central constriction of six apolar residues has been shown to form a seal, but also to determine the hydrophobicity threshold for membrane integration: Mutation of these residues in yeast Sec61p to glycines, serines, aspartates, or lysines lowered the hydrophobicity required for integration; mutation to alanines increased it. Whereas four leucines distributed in an oligo-alanine H segment were sufficient for 50% integration, we now find four leucines in the N-terminal half of the H segment to produce significantly more integration than in the C-terminal half, suggesting functional asymmetry within the translocon. Scanni"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Functional asymmetry within the Sec61p translocon."],"pmcid":["PMC3839696"],"funding_grant_id":["144111","139205"],"pubmed_authors":["Baday S","Berneche S","Junne T","Spiess M","Demirci E"],"additional_accession":[]},"is_claimable":false,"name":"Functional asymmetry within the Sec61p translocon.","description":"The Sec61 translocon forms a pore to translocate polypeptide sequences across the membrane and offers a lateral gate for membrane integration of hydrophobic (H) segments. A central constriction of six apolar residues has been shown to form a seal, but also to determine the hydrophobicity threshold for membrane integration: Mutation of these residues in yeast Sec61p to glycines, serines, aspartates, or lysines lowered the hydrophobicity required for integration; mutation to alanines increased it. Whereas four leucines distributed in an oligo-alanine H segment were sufficient for 50% integration, we now find four leucines in the N-terminal half of the H segment to produce significantly more integration than in the C-terminal half, suggesting functional asymmetry within the translocon. Scanni","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Nov","modification":"2026-05-02T01:18:48.768Z","creation":"2019-03-27T03:09:14Z"},"accession":"S-EPMC3839696","cross_references":{"pubmed":["24191046"],"doi":["10.1073/pnas.1318432110"]}}