Interaction of actin and its 11-amino acid C-terminal peptide as cofactors with the adenovirus proteinase.
Actin bound to the adenovirus proteinase (AVP) with a lower equilibrium dissociation constant, 4.2 nM, than those exhibited by two viral, nuclear cofactors for AVP, the 11-amino acid peptide pVIc and the viral DNA. The k(cat)/K(m) ratio for substrate hydrolysis by AVP increased 150,000-fold in the presence of actin. The 11-amino acid residue peptide corresponding to the C-terminus of actin, which is highly homologous to pVIc, bound to AVP and stimulated its activity in the presence of DNA. As a cellular cofactor for AVP, AVP(actin) complexes may facilitate the cleavage of cytoskeletal proteins, preparing the infected cell for lysis and release of nascent virions.
Brown
Mark T
MT
Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.
Mangel
Walter F
WF
D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000256:Adenoviridae / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*
D000199:Actins; D004279:DNA, Viral; D010446:Peptide Fragments; D014764:Viral Proteins; D003546:Cysteine Endopeptidases