The substrate specificity of the protein kinase induced in cells infected with herpesviruses: Studies with synthetic substatres indicate structural requirements distinct from other protein kinases |
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| Institution: | 1. Department of Biochemistry, University of Glasgow, Glasgow G12 8QQ U.K.;2. Istituto di Chimica Biologica dell''Universita, Via F. Marzolo 3, 35131 Padova Italy;3. Dipartimento di Chimica Organica dell''Universita, Padova Italy;1. Unidad de Dermatología Médico-Quirúrgica y Venereología, Hospital Comarcal Santa Ana, Motril, España;2. Unidad de Gestión Clínica de Dermatología y Venereología, Complejo Hospitalario Universitario de Granada, Granada, España;1. Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea;2. Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea;3. Department of Functional Genomics, KRIBB School of Bioscience, Korea University of Science and Technology (UST), Daejeon 34141, Republic of Korea;1. Federal University of Ceará – UFC, Fortaleza, CE, Brazil;2. Oswaldo Cruz Foundation - Fiocruz, Fortaleza, CE, Brazil;3. Regional University of Cariri – URCA, Microbiology and Molecular Biology Laboratory – LMBM, Crato, CE, Brazil;1. School of Biology, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, United Kingdom;2. Kcat Enzymatic Private Limited, Bangalore, India;1. Department of Nutritional Sciences, University of Wisconsin, Madison, Wisconsin;2. Department of Surgery, University of Wisconsin, Madison, Wisconsin;3. Department of Internal Medicine, School of Medicine, Yale University, New Haven, Connecticut;4. Department of Cell Biology, School of Medicine, Yale University, New Haven, Connecticut;5. Veterans Administration Connecticut Healthcare, West Haven, Connecticut;1. State Key Laboratory of Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China;2. National Institute of Biological Sciences, Number 7 Science Park Road, Zhongguancun Life Science Park, Beijing 102206, China |
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| Abstract: | Synthetic peptides have been used to investigate the site specificity of highly purified virus induced protein kinase, a recently discovered protein kinase isolated from cells infected with α-herpesviruses. The enzyme from cells infected with pseudorabies virus can catalyse the phosphorylation of both seryl and threonyl residues in peptides that contain several arginyl residues on the amino-terminal side of the target residue. At least two arginyl residues are required, and the best substrates examined contain four to six such residues. Virus induced protein kinase differs in site specificity from protein kinase C in being unable to phosphorylate peptides in which multiple arginyl residues are on the carboxyl-terminal side of the target residue, or to phosphorylate peptides in which the arginyl residues are replaced by ornithyl residues. Virus induced protein kinase from cells infected with herpes simples virus type I had similar substrate preferences to virus induced protein kinase from cells infected with pseudorabies virus. Although virus induced protein kinase and the cyclic AMP-dependent protein kinase have several peptide substrates in common, their relative preferences for these (as indicated by Km values) were found to be very different. |
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