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Interaction of actin and its 11‐amino acid C‐terminal peptide as cofactors with the adenovirus proteinase
Author(s) -
Brown Mark T,
Mangel Walter F
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00285-6
Subject(s) - peptide , cofactor , actin , biochemistry , amino acid , cleavage (geology) , chemistry , peptide sequence , proteolysis , lysis , dna , enzyme , biology , microbiology and biotechnology , paleontology , fracture (geology) , gene
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.