Abstract
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.
MeSH Terms
Amino Acid Sequence
Capsid/genetics,metabolism
Capsid Proteins
Coliphages/genetics
Escherichia coli/genetics
Membrane Proteins/genetics,metabolism
Mutation
Oligodeoxyribonucleotides
Plasmids
Chemicals
Capsid Proteins
Membrane Proteins
Oligodeoxyribonucleotides
coat protein, Bacteriophage M13
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kuhn A
Kreil G
Wickner W
References (24)
24 references, click to expand
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