Structural basis of the association of HIV-1 matrix protein with DNA

PLoS One. 2010 Dec 23;5(12):e15675. doi: 10.1371/journal.pone.0015675.


HIV-1 matrix (MA) is a multifunctional protein that is synthesized as a polyprotein that is cleaved by protease during viral maturation. MA contains a cluster of basic residues whose role is controversial. Proposed functions include membrane anchoring, facilitating viral assembly, and directing nuclear import of the viral DNA. Since MA has been reported to be a component of the preintegration complex (PIC), we have used NMR to probe its interaction with other PIC components. We show that MA interacts with DNA and this is likely sufficient to account for its association with the PIC.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Base Sequence
  • Calorimetry / methods
  • DNA / chemistry
  • DNA / genetics*
  • DNA, Viral / genetics*
  • Escherichia coli / metabolism
  • HIV-1 / genetics*
  • Human Immunodeficiency Virus Proteins / chemistry
  • Magnetic Resonance Spectroscopy / methods
  • Molecular Sequence Data
  • Oligonucleotides / genetics
  • Phenotype
  • Polyproteins / chemistry
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA / chemistry


  • DNA, Viral
  • Human Immunodeficiency Virus Proteins
  • Oligonucleotides
  • Polyproteins
  • RNA
  • DNA