title: Evidence that a phage T4 DNA packaging enzyme is a processed form of the major capsid gene product.
abstract: A phage T4 DNA packaging enzyme appears to arise as a processed form of the major T4 capsid structural protein gp23. The enzyme activity and antigen are missing from all head gene mutants that block the morphogenetic proteolytic processing reactions of the head proteins in vivo. The enzyme antigen can be formed in vitro by T4 (gp21) specific processing of gp23 containing extracts. Enzyme antigen is found in active processed proheads but not in full heads. The enzyme and the major capsid protein show immunological cross-reactivity, produce common peptides upon proteolysis, and share an assembly-conformation-dependent ATP binding site. The packaging enzyme and the mature capsid protein (gp23*) both appear to arise from processing of gp23, the former as a minor product of a specific gp23 structure in the prohead, acting in DNA packaging as a DNA-dependent ATPase, and a headful-dependent terminase.
authors.forename: V B
authors.initials: VB
authors.lastname: Rao
authors.forename: L W
authors.initials: LW
authors.lastname: Black
mesh_terms: D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites; D002213:Capsid / Q000235:genetics*; D003429:Cross Reactions; D004265:DNA Helicases; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005796:Genes; D005814:Genes, Viral; D007106:Immune Sera; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity; D013604:T-Phages / Q000201:enzymology / Q000235:genetics*
chemical_list: D007106:Immune Sera; D000251:Adenosine Triphosphatases; D004265:DNA Helicases