Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication

Trends Biochem Sci. 1998 Aug;23(8):297-301. doi: 10.1016/s0968-0004(98)01256-0.

Abstract

Retrovirus particles contain a small, basic protein, the nucleocapsid (NC) protein, that possesses 'nucleic acid chaperone' activity--that is, the NC protein can catalyze the rearrangement of a nucleic acid molecule into the conformation that has the maximal number of base pairs. The molecular mechanism that underlies this effect is not understood. Because the chaperone activity is apparently crucial during the infectious process, NC is a potential target for antiviral therapy.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Gene Products, gag / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acids / metabolism*
  • Nucleocapsid Proteins / chemistry*
  • Nucleocapsid Proteins / genetics
  • Nucleocapsid Proteins / metabolism*
  • Protein Conformation
  • RNA, Viral / genetics
  • RNA, Viral / metabolism
  • RNA-Directed DNA Polymerase / genetics
  • RNA-Directed DNA Polymerase / metabolism
  • Retroviridae / genetics*
  • Virus Replication*

Substances

  • Gene Products, gag
  • Nucleic Acids
  • Nucleocapsid Proteins
  • RNA, Viral
  • RNA-Directed DNA Polymerase