Identification and characterization of serine/threonine protein kinase activity intrinsic to the L protein of vesicular stomatitis virus New Jersey
| Autor: | Boyd E. Haley, David C. Hammond, Judith A. Lesnaw |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Serine/threonine-specific protein kinase
Azides Affinity Labels Serine threonine protein kinase DNA-Directed RNA Polymerases Vesiculovirus Biology Protein Serine-Threonine Kinases Receptor protein serine/threonine kinase RNA-Dependent RNA Polymerase Virology Molecular biology AKT3 MAP2K7 Kinetics Viral Proteins Adenosine Triphosphate Biochemistry Phosphorylation Threonine Protein kinase A Protein Kinases |
| Zdroj: | The Journal of general virology. 73 |
| ISSN: | 0022-1317 |
| Popis: | A photoaffinity analogue of ATP, 8-azido-adenosine 5'-triphosphate (8-N3ATP), was used to probe ATP-binding sites in native transcription complexes of vesicular stomatitis virus (VSV) (New Jersey serotype). The analogue was found to be a substrate for a serine/threonine protein kinase that phosphorylated both the NS and L proteins of native complexes. The analogue failed to interact with the RNA polymerase, another ATP-utilizing activity associated with the transcription complex. Kinetic analyses of both ATP and 8-N3ATP utilization by the protein kinase yielded biphasic saturation curves. Photolysis of 8-N3ATP in the presence of VSV transcription complexes resulted in selective labelling of the L protein. The photolabelling of L was saturable and apparently biphasic. Photolabelling of the L protein was significantly reduced by competition with ATP whereas other nucleoside triphosphates (GTP, UTP and CTP) were ineffective competitors. The stoichiometry of photolabelling was 0.2 at 10 microM-8N3ATP and 1.3 at 100 microM-ATP. These data provide chemical evidence for a virus-encoded serine/threonine protein kinase which resides on the L protein. |
| Databáze: | OpenAIRE |
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