Heterogeneity of the procapsid of bacteriophage T3

J Virol. 1985 Jul;55(1):232-7. doi: 10.1128/JVI.55.1.232-237.1985.

Abstract

Like other double-stranded DNA bacteriophages, bacteriophage T3 assembles a DNA-free procapsid that subsequently packages the bacteriophage DNA. By agarose gel electrophoresis, it has been found that the T3 procapsid has a negative electrophoretic mobility (mu) that progressively increases in magnitude by as much as 3% after assembly of the procapsid. This increase is (i) caused by an increase in the solid support-free mu (muo) of the procapsid, not a decrease in its radius, and (ii) not prevented by either genetically or chemically (use of proflavine) blocking DNA packaging. However, inhibition of the formation of high-energy compounds with a mixture of cyanide and fluoride ions does block the time-dependent increase in the magnitude of muo. This increase appears to be accompanied by addition of an unidentified T3 protein to the procapsid.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Capsid / metabolism*
  • DNA, Viral / metabolism
  • Electrophoresis, Agar Gel
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Weight
  • Morphogenesis
  • Oxidation-Reduction
  • Potassium Cyanide / pharmacology
  • Proflavine / pharmacology
  • Protein Processing, Post-Translational
  • Sodium Fluoride / pharmacology
  • T-Phages / metabolism
  • T-Phages / ultrastructure*
  • Time Factors

Substances

  • DNA, Viral
  • Sodium Fluoride
  • Proflavine
  • Potassium Cyanide