Skip to main content
NCBI home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1978 Jun;5(6):1947–1954. doi: 10.1093/nar/5.6.1947

Binding of tRNA nucleotidyltransferase to Affi-Gel Blue: rapid purification of the enzyme and binding studies.

M P Deutscher, P Masiakowski
PMCID: PMC342136  PMID: 673841

Abstract

Rabbit liver tRNA nucleotidyldransferase bound to columns of Affi-Gel Blue and could be specifically eluted with tRNA. This observation led to development of a rapid purification procedure for the enzyme. The adsorbent was also used to assess interaction of tRNA nucleotidyltransferase with various polynucleotides and substrates. The enzyme could be efficiently desorbed from Affi-Gel Blue by low concentrations of tRNA-C-C, less well by tRNA-C-C-A, and not at all by poly(A), poly(C), ATP or CTP.

Full text

PDF
1947

Selected References

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

  1. De Maeyer-Guignard J., Thang M. N., De Maeyer E. Binding of mouse interferon to polynucleotides. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3787–3790. doi: 10.1073/pnas.74.9.3787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Deutscher M. P., Foulds J., McClain W. H. Transfer ribonucleic acid nucleotidyl-transferase plays an essential role in the normal growth of Escherichia coli and in the biosynthesis of some bacteriophage T4 transfer ribonucleic acids. J Biol Chem. 1974 Oct 25;249(20):6696–6699. [PubMed] [Google Scholar]
  3. Deutscher M. P., Hilderman R. H. Isolation and partial characterization of Escherichia coli mutants with low levels of transfer ribonucleic acid nucleotidyltransferase. J Bacteriol. 1974 May;118(2):621–627. doi: 10.1128/jb.118.2.621-627.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Deutscher M. P., Lin J. J., Evans J. A. Transfer RNA metabolism in Escherichia coli cells deficient in tRNA nucleotidyltransferase. J Mol Biol. 1977 Dec 25;117(4):1081–1094. doi: 10.1016/s0022-2836(77)80014-4. [DOI] [PubMed] [Google Scholar]
  5. Deutscher M. P. Rabbit liver tRNA nucleotidyltransferase. Methods Enzymol. 1974;29:706–716. doi: 10.1016/0076-6879(74)29063-3. [DOI] [PubMed] [Google Scholar]
  6. Deutscher M. P. Reactions at the 3' terminus of transfer ribonucleic acid. 3. Catalytic properties of two purified rabbit liver transfer ribonucleic acid nucleotidyl transferases. J Biol Chem. 1972 Jan 25;247(2):459–468. [PubMed] [Google Scholar]
  7. Deutscher M. P. Reactions at the 3' terminus of transfer ribonucleic acid. II. Purification and physical and chemical properties of rabbit liver transfer ribonucleic acid nucleotidyltransferase. J Biol Chem. 1972 Jan 25;247(2):450–458. [PubMed] [Google Scholar]
  8. Deutscher M. P. Reactions of the 3' terminus of transfer ribonucleic acid. VI. Properties of the poly(C) polymerase activity associated with rabbit liver transfer ribonucleic acid nucleotidyltransferase. J Biol Chem. 1973 May 10;248(9):3108–3115. [PubMed] [Google Scholar]
  9. Deutscher M. P. Synthesis and functions of the -C-C-A terminus of transfer RNA. Prog Nucleic Acid Res Mol Biol. 1973;13:51–92. doi: 10.1016/s0079-6603(08)60100-2. [DOI] [PubMed] [Google Scholar]
  10. Drocourt J. L., Thang D. C., Thang M. N. Blue-dextran--Sepharose affinity chromatography: recognition of a polynucleotide binding site of a protein. Eur J Biochem. 1978 Jan 16;82(2):355–362. doi: 10.1111/j.1432-1033.1978.tb12030.x. [DOI] [PubMed] [Google Scholar]
  11. Goodman H. M., Olson M. V., Hall B. D. Nucleotide sequence of a mutant eukaryotic gene: the yeast tyrosine-inserting ochre suppressor SUP4-o. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5453–5457. doi: 10.1073/pnas.74.12.5453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Masiakowski P., Deutscher M. P. The dinucleoside monophosphate, CpC, is a model acceptor substrate for rabbit-liver tRNA nucleotidyltransferase. FEBS Lett. 1977 May 15;77(2):261–264. doi: 10.1016/0014-5793(77)80247-0. [DOI] [PubMed] [Google Scholar]
  13. Moe J. G., Piszkiewicz D. Purification of isoleucyl transfer ribonucleic acid synthetase by affinity chromatography on blue dextran-sepharose. FEBS Lett. 1976 Dec 15;72(1):147–150. doi: 10.1016/0014-5793(76)80832-0. [DOI] [PubMed] [Google Scholar]
  14. Schofield P., Williams K. R. Purification and some properties of Escherichia coli tRNA nucleotidyltransferase. J Biol Chem. 1977 Aug 10;252(15):5584–5588. [PubMed] [Google Scholar]
  15. Sprinzl M., Sternbach H., von der Haar F., Cramer F. Enzymatic incorporation of ATP and CTP analogues into the 3' end of tRNA. Eur J Biochem. 1977 Dec;81(3):579–589. doi: 10.1111/j.1432-1033.1977.tb11985.x. [DOI] [PubMed] [Google Scholar]
  16. Sternbach H., von der Haar F., Schlimme E., Gaertner E., Cramer F. Isolation and properties of tRNA nucleotidyl transferase from yeast. Eur J Biochem. 1971 Sep 24;22(2):166–172. doi: 10.1111/j.1432-1033.1971.tb01528.x. [DOI] [PubMed] [Google Scholar]
  17. Thang M. N., De Maeyer-Guignard J., De Maeyer E. Interaction of interferon with tRNA. FEBS Lett. 1977 Aug 15;80(2):365–370. doi: 10.1016/0014-5793(77)80477-8. [DOI] [PubMed] [Google Scholar]
  18. Thompson S. T., Cass K. H., Stellwagen E. Blue dextran-sepharose: an affinity column for the dinucleotide fold in proteins. Proc Natl Acad Sci U S A. 1975 Feb;72(2):669–672. doi: 10.1073/pnas.72.2.669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wilson J. E. Applications of blue dextran and Cibacron Blue F3GA in purification and structural studies of nucleotide-requiring enzymes. Biochem Biophys Res Commun. 1976 Oct 4;72(3):816–823. doi: 10.1016/s0006-291x(76)80206-9. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES