A covalent complex between retroviral integrase and nicked substrate DNA.
AUTOR(ES)
Katzman, M
RESUMO
Purified retroviral integrase (IN) from avian sarcoma-leukosis viruses can appropriately process the termini of linear viral DNA, cleave host DNA in a sequence-independent manner, and catalyze integrative recombination; an exogenous source of energy is not required for these reactions. Using DNA substrates containing radioactive phosphate groups, we demonstrate that IN becomes covalently joined to the new 5' phosphate ends of DNA produced at sites of cleavage. Most of the phosphodiester linkages between IN and DNA involve serine, but some involve threonine. Computer-assisted alignment of 80 retroviral and retrotransposon IN sequences identified one serine that is conserved in all of these proteins and three less-conserved threonine residues. These results identify candidate active-site residues and provide support for the participation of a covalent IN-DNA intermediate in retroviral integration.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=51732Documentos Relacionados
- Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA.
- Substrate Sequence Selection by Retroviral Integrase
- Structure of a nicked DNA-protein complex isolated from simian virus 40: covalent attachment of the protein to DNA and nick specificity.
- Chemical and enzymatic analysis of covalent bonds between peptides and chromosomal DNA.
- Molecular structure of nicked DNA: a substrate for DNA repair enzymes.
