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Both hydrophobic domains of M13 procoat are required to initiate membrane insertion.
Author(s) -
Kuhn A.,
Kreil G.,
Wickner W.
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04699.x
Subject(s) - biology , membrane protein , membrane , genetics , microbiology and biotechnology
M13 procoat protein has two hydrophobic domains, one in the leader peptide and one which anchors the mature coat protein in the membrane. Disruption of the membrane anchor region by insertion of arginyl residues does not yield periplasmic coat protein. Instead, the rate of membrane assembly is slowed greater than 100‐fold (t1/2 less than 5 s for wild‐type, t1/2 greater than 10 min for mutant). The hydrophobic region of mature coat protein not only functions as a membrane anchor, but has an important role in the membrane assembly process per se.