Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1978 Oct 1;175(1):189–192. doi: 10.1042/bj1750189

Intrasubunit nucleotide binding in ribonucleic acid polymerase.

A D Malcolm, J R Moffatt
PMCID: PMC1186053  PMID: 216347

Abstract

1. Periodate oxidation of the ribose ring was used to synthesize derivatives of nucleoside triphosphates. 2. These oxidized nucleoside triphosphates. 2. These oxidized nucleoside triphosphates are competitive inhibitors of RNA polymerase. 3. On incubation, together with NaBH4, these oxidized labelled nucleotides are covalently bound to Escherichia coli RNA polymerase. 4. Nucleoside triphosphate substrates decrease the extent of labelling. 5. A lysine residue in an alpha-subunit is labelled. 6. The significance of these results in relation to the location of the nucleotide-binding site is discussed.

Full text

PDF
189

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anthony D. D., Goldthwait D. A., Wu C. W. Studies with the ribonucleic acid polymerase. II. Kinetic aspects of initiation and polymerization. Biochemistry. 1969 Jan;8(1):246–256. doi: 10.1021/bi00829a035. [DOI] [PubMed] [Google Scholar]
  2. Armstrong V. W., Sternbach H., Eckstein F. Affinity labeling of Escherichia coli DNA-dependent RNA polymerase with 5-formyl-l-(alpha-D-ribofuranosyl)uracil 5'-triphosphate. Biochemistry. 1976 May 18;15(10):2086–2091. doi: 10.1021/bi00655a009. [DOI] [PubMed] [Google Scholar]
  3. Armstrong V. W., Sternbach H., Eckstein F. Modification of an essential arginine in Escherichia coli DNA-dependent RNA polymerase. FEBS Lett. 1976 Nov;70(1):48–50. doi: 10.1016/0014-5793(76)80723-5. [DOI] [PubMed] [Google Scholar]
  4. Burgess R. R., Jendrisak J. J. A procedure for the rapid, large-scall purification of Escherichia coli DNA-dependent RNA polymerase involving Polymin P precipitation and DNA-cellulose chromatography. Biochemistry. 1975 Oct 21;14(21):4634–4638. doi: 10.1021/bi00692a011. [DOI] [PubMed] [Google Scholar]
  5. Coggins J. R., Lumsden J., Malcolm A. D. A study of the quaternary structure of Escherichia coli RNA polymerase using bis(imido esters). Biochemistry. 1977 Mar 22;16(6):1111–1116. doi: 10.1021/bi00625a013. [DOI] [PubMed] [Google Scholar]
  6. Downey K. M., So A. G. Studies on the kinetics of ribonucleic acid chain initiation and elongation. Biochemistry. 1970 Jun 9;9(12):2520–2525. doi: 10.1021/bi00814a019. [DOI] [PubMed] [Google Scholar]
  7. Easterbrook-Smith S. B., Wallace J. C., Keech D. B. Pyruvate carboxylase: affinity labelling of the magnesium adenosine triphosphate binding site. Eur J Biochem. 1976 Feb 2;62(1):125–130. doi: 10.1111/j.1432-1033.1976.tb10105.x. [DOI] [PubMed] [Google Scholar]
  8. Frischauf A. M., Scheit K. H. Affinity labeling of E. coli RNA polymerase with substrate and template analogues. Biochem Biophys Res Commun. 1973 Aug 21;53(4):1227–1233. doi: 10.1016/0006-291x(73)90596-2. [DOI] [PubMed] [Google Scholar]
  9. Goff C. G. Chemical structure of a modification of the Escherichia coli ribonucleic acid polymerase alpha polypeptides induced by bacteriophage T4 infection. J Biol Chem. 1974 Oct 10;249(19):6181–6190. [PubMed] [Google Scholar]
  10. Graham A., Greene J., Lowe P. A., Malcolm A. D. Binding sites on Escherichia coli ribonucleic acid polymerase. Biochem Soc Trans. 1976;4(4):633–634. doi: 10.1042/bst0040633. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Mailhammer R., Yang H. L., Reiness G., Zubay G. Effects of bacteriophage T4-induced modification of Escherichia coli RNA polymerase on gene expression in vitro. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4928–4932. doi: 10.1073/pnas.72.12.4928. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Malcom A. D., Mitchell G. J., Wasylyk B. The activation of RNA polymerase by alkylammonium ions. Nucleic Acids Res. 1975 Apr;2(4):537–544. doi: 10.1093/nar/2.4.537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nicholson B. H., King A. M. Thiol function and tertiary structure of RNA polymerase of Escherichia coli. Eur J Biochem. 1973 Sep 3;37(3):575–584. doi: 10.1111/j.1432-1033.1973.tb03021.x. [DOI] [PubMed] [Google Scholar]
  15. Nixon J., Spoor T., Evans J., Kimball A. Affinity labeling of Escherichia coli B deoxyribonucleic acid dependent ribonucleic acid polymerase. Biochemistry. 1972 Nov 21;11(24):4570–4573. doi: 10.1021/bi00774a023. [DOI] [PubMed] [Google Scholar]
  16. Ovchinnikov Y. A., Lipkin V. M., Modyanov N. N., Chertov O. Y., Smirnov Y. V. Primary structure of alpha-subunit of DNA-dependent RNA polymerase from Escherichia coli. FEBS Lett. 1977 Apr 1;76(1):108–111. doi: 10.1016/0014-5793(77)80131-2. [DOI] [PubMed] [Google Scholar]
  17. Powell J. T., Brew K. Affinity labeling of bovine colostrum galactosyltransferase with a uridine 5'-diphosphate derivative. Biochemistry. 1976 Aug 10;15(16):3499–3505. doi: 10.1021/bi00661a016. [DOI] [PubMed] [Google Scholar]
  18. Seifert W., Rabussay D., Zillig W. On the chemical nature of alteration and modification of DNA dependent RNA polymerase of E. coli after T4 infection. FEBS Lett. 1971 Aug 15;16(3):175–179. doi: 10.1016/0014-5793(71)80125-4. [DOI] [PubMed] [Google Scholar]
  19. Travers A. RNA polymerase specificity and the control of growth. Nature. 1976 Oct 21;263(5579):641–646. doi: 10.1038/263641a0. [DOI] [PubMed] [Google Scholar]
  20. Venegas A., Martial J., Valenzuela P. Active site-directed inhibition of E. coli DNA-dependent RNA polymerase by pyridoxal 5'-phosphate. Biochem Biophys Res Commun. 1973 Dec 19;55(4):1053–1059. doi: 10.1016/s0006-291x(73)80001-4. [DOI] [PubMed] [Google Scholar]
  21. Wasylyk B., Malcolm A. D. Chemical modification of ribonucleic acid polymerase with N-bromosuccinimide. Biochem Soc Trans. 1975;3(5):654–654. doi: 10.1042/bst0030654. [DOI] [PubMed] [Google Scholar]
  22. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  23. Wu C. W., Goldthwait D. A. Studies of nucleotide binding to the ribonucleic acid polymerase by a fluoresence technique. Biochemistry. 1969 Nov;8(11):4450–4458. doi: 10.1021/bi00839a034. [DOI] [PubMed] [Google Scholar]
  24. Wu F. Y., Wu C. W. Fluorescent affinity labeling of initiation site on ribonucleic acid polymerase of Escherichia coli. Biochemistry. 1974 Jun 4;13(12):2562–2566. doi: 10.1021/bi00709a014. [DOI] [PubMed] [Google Scholar]
  25. Yarbrough L. R., Wu C. W. Role of sulfhydryl residues of Escherichia coli ribonucleic acid polymerase in template recognition and specific initiation. J Biol Chem. 1974 Jul 10;249(13):4079–4085. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES