Protein kinase of bacteriophage T7. 2. Properties, enzyme synthesis in vitro and regulation of enzyme synthesis and activity in vivo
Protein kinase, which was isolated from cells infected with T7, is indeed a viral gene product. This is shown by DNA-dependent synthesis in vitro. The protein kinase transfers phosphate from ATP to seryl or threonyl residues in protein. The enzyme has only a relative requirement for magnesium ions,...
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| Veröffentlicht in: | European journal of biochemistry 1975-06, Vol.55 (1), p.305-314 |
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| container_start_page | 305 |
| container_title | European journal of biochemistry |
| container_volume | 55 |
| creator | Pai, S H Rahmsdorf, H J Ponta, H Hirsch-Kauffmann, M Herrlich, P Schweiger, M |
| description | Protein kinase, which was isolated from cells infected with T7, is indeed a viral gene product. This is shown by DNA-dependent synthesis in vitro. The protein kinase transfers phosphate from ATP to seryl or threonyl residues in protein. The enzyme has only a relative requirement for magnesium ions, but is only active at low ionic strength. The best substrate is lysozyme. T7 protein kinase activity is not stimulated by cyclic 3':5'-AMP and/or cyclic 3':5'-GMP. The T7 protein kinase carries -- SH groups essential for activity. There is indication that the enzyme phosphorylates itself and causes self inactivation, which may explain the fast disappearance of enzyme activity in vivo. Bacteriophage T3 also induces a protein kinase which is similar to the T7-induced enzyme in all respects tested. |
| doi_str_mv | 10.1111/j.1432-1033.1975.tb02164.x |
| format | Article |
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There is indication that the enzyme phosphorylates itself and causes self inactivation, which may explain the fast disappearance of enzyme activity in vivo. 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Properties, enzyme synthesis in vitro and regulation of enzyme synthesis and activity in vivo</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Protein kinase, which was isolated from cells infected with T7, is indeed a viral gene product. This is shown by DNA-dependent synthesis in vitro. The protein kinase transfers phosphate from ATP to seryl or threonyl residues in protein. The enzyme has only a relative requirement for magnesium ions, but is only active at low ionic strength. The best substrate is lysozyme. T7 protein kinase activity is not stimulated by cyclic 3':5'-AMP and/or cyclic 3':5'-GMP. The T7 protein kinase carries -- SH groups essential for activity. There is indication that the enzyme phosphorylates itself and causes self inactivation, which may explain the fast disappearance of enzyme activity in vivo. Bacteriophage T3 also induces a protein kinase which is similar to the T7-induced enzyme in all respects tested.</description><subject>Ammonium Chloride - pharmacology</subject><subject>Cations, Divalent</subject><subject>Coliphages - enzymology</subject><subject>DNA Viruses - enzymology</subject><subject>Escherichia coli - enzymology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Magnesium - pharmacology</subject><subject>Protamine Kinase - biosynthesis</subject><subject>Protamine Kinase - metabolism</subject><subject>Protein Kinases - metabolism</subject><subject>Sulfhydryl Compounds - pharmacology</subject><subject>Temperature</subject><subject>Transcription, Genetic</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkT1PwzAURS3EVyn8AwaLgYmEZztxGjZU8SVVgqHMlpO8tC5tXGy3apn54SRq1QUvtuRz3pPuJeSGQczacz-LWSJ4xECImOVZGocCOJNJvDkivcPXMekBsCTieSrPyYX3MwCQuczOyClP2lfaI78fzgY0Df0yjfZIbU0LXQZ0xi6neoJ0nMWUx7TFluiCQX9HsfnZLpD6bROm6I2nrb42wVmqm4o6nKzmOhjbdMP-sR3SLjCtsN2Ja3tJTmo993i1v_vk8_lpPHyNRu8vb8PHUVSyjIVooEsoONQZq2tRoOQIXEotRaYZYM0SyXOOVYpVDjqtuCjzLC8TiQXTBdRc9Mntbu7S2e8V-qAWxpc4n-sG7cqrgQBIBXTgww4snfXeYa2Wziy02yoGqmtAzVQXs-piVl0Dat-A2rTy9X7LqlhgdVB3kYs_aVSFfA</recordid><startdate>19750616</startdate><enddate>19750616</enddate><creator>Pai, S H</creator><creator>Rahmsdorf, H J</creator><creator>Ponta, H</creator><creator>Hirsch-Kauffmann, M</creator><creator>Herrlich, P</creator><creator>Schweiger, M</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19750616</creationdate><title>Protein kinase of bacteriophage T7. 2. 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Properties, enzyme synthesis in vitro and regulation of enzyme synthesis and activity in vivo</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1975-06-16</date><risdate>1975</risdate><volume>55</volume><issue>1</issue><spage>305</spage><epage>314</epage><pages>305-314</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Protein kinase, which was isolated from cells infected with T7, is indeed a viral gene product. This is shown by DNA-dependent synthesis in vitro. The protein kinase transfers phosphate from ATP to seryl or threonyl residues in protein. The enzyme has only a relative requirement for magnesium ions, but is only active at low ionic strength. The best substrate is lysozyme. T7 protein kinase activity is not stimulated by cyclic 3':5'-AMP and/or cyclic 3':5'-GMP. The T7 protein kinase carries -- SH groups essential for activity. 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| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1975-06, Vol.55 (1), p.305-314 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Ammonium Chloride - pharmacology Cations, Divalent Coliphages - enzymology DNA Viruses - enzymology Escherichia coli - enzymology Hydrogen-Ion Concentration Kinetics Magnesium - pharmacology Protamine Kinase - biosynthesis Protamine Kinase - metabolism Protein Kinases - metabolism Sulfhydryl Compounds - pharmacology Temperature Transcription, Genetic |
| title | Protein kinase of bacteriophage T7. 2. Properties, enzyme synthesis in vitro and regulation of enzyme synthesis and activity in vivo |
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