title: Mutants at conserved positions in gene IV, a gene required for assembly and secretion of filamentous phages.
abstract: The filamentous phage protein pIV is required for assembly and secretion of the virus and possesses regions homologous to those found in a number of Gram-negative bacterial proteins that are essential components of a widely distributed extracellular protein-export system. These proteins form multimers that may constitute an outer membrane channel that allows phage/protein egress. Three sets of f1 gene IV mutants were isolated at positions that are absolutely (G355 and P375) or largely (F381) conserved amongst the 16 currently known family members. The G355 mutants were non-functional, interfered with assembly of pIV+ phage, and made Escherichia coli highly sensitive to deoxycholate. The P375 mutants were non-functional and defective in multimerization. Many of the F381 mutants retained substantial function, and even those in which charged residues had been introduced supported some phage assembly. Some inferences about the roles of these conserved amino acids are made from the mutant phenotypes.
authors: Rockefeller University, New York, New York 10021.
authors: M
authors: M
authors: Russel
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003090:Coliphages / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D003840:Deoxycholic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics*; D015870:Gene Expression; D005814:Genes, Viral; D008969:Molecular Sequence Data; D009154:Mutation; D009876:Operon; D010641:Phenotype; D016415:Sequence Alignment; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics*
chemical_list: D014764:Viral Proteins; D003840:Deoxycholic Acid