title: Bacteriophage Mu head assembly.
abstract: The protein composition of defective particles produced by various bacteriophage Mu head-gene mutants was analyzed by SDS-PAGE. An abundant 20-kDa protein was detected in only one type of defective head. This protein exhibits properties of a scaffolding protein. A 50-kDa structural protein present in most defective heads was shown to be produced by cleavage of the C-terminus of the 64-kDa polypeptide encoded by gene H. Cleavage occurs during head assembly at a site which, according to earlier results, might separate two different functional domains in gpH. A fraction of the gpH molecules produced upon Mu induction sediment in a 25 S complex, suggesting that gpH participates in the formation of an early intermediate of Mu head assembly. Characteristics of gpH suggest that it may be the Mu portal protein.
authors.affiliation: Laboratoire de Génétique des Procaryotes, Unité Transposition Bactérienne, Université Libre de Bruxelles, Belgium.
authors.forename: R
authors.initials: R
authors.lastname: Grimaud
mesh_terms: D010583:Bacteriophage mu / Q000502:physiology*; D002499:Centrifugation, Density Gradient; D003673:Defective Viruses / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D014764:Viral Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D019065:Virus Assembly
chemical_list: D014764:Viral Proteins