Both hydrophobic domains of M13 procoat are required to initiate membrane insertion.
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.
D000595:Amino Acid Sequence; D002213:Capsid / Q000235:genetics / Q000378:metabolism*; D036022:Capsid Proteins; D003090:Coliphages / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009838:Oligodeoxyribonucleotides; D010957:Plasmids
D036022:Capsid Proteins; D008565:Membrane Proteins; D009838:Oligodeoxyribonucleotides; C025668:coat protein, Bacteriophage M13