title: The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domain.
abstract: The M13 coat protein spans the Escherichia coli plasma membrane with its amino-terminus facing the periplasm. It is made as a precursor--the procoat--with a typical leader peptide. Mutations which destroy the basic character of the carboxy-terminal domain of procoat, a domain which is oriented towards the cytoplasm, block membrane assembly, while insertion of three lysyl residues near the carboxy terminus partially restores assembly. Thus the information specifying membrane insertion of M13 procoat protein is found in its mature region as well as the leader and is not simply decoded in an amino to carboxy direction.
mesh_terms: D000595:Amino Acid Sequence; D001692:Biological Transport; D002213:Capsid / Q000235:genetics / Q000378:metabolism*; D036022:Capsid Proteins; D002462:Cell Membrane / Q000378:metabolism*; D003090:Coliphages / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
chemical_list: D036022:Capsid Proteins; D011498:Protein Precursors; C025668:coat protein, Bacteriophage M13