A study of some molecular and kinetic properties of two tRNA methyltransferases from mouse plasmocytoma.

Abstract

A tRNA(adenine-1)methyltransferase and a tRNA(cytosine-5)methyltransferase have been partially purified from mouse plasmocytoma MOPC 173. Their apparent Mr are 200000-230000 and 110000-140000, respectively, as determined by gel filtration and density gradient centrifugation. Both enzymes exhibit maximum activity in the presence of high concentrations of monovalent cations (0.175 M and 0.25 M KCl, respectively) and in the absence of magnesium. Their kinetic constants have been determined at various KCl concentrations, with several tRNA species as substrates. These constants may differ by more than one order of magnitude, depending upon the substrate used, and they are strongly dependent upon the ionic concentration as well. The possibility that the tRNA(adenine-1)methyltransferase from mouse plasmocytoma is different from the homologous enzyme purified from a normal rat tissue [Glick, J. M. and Leboy, P. S. (1977) J. Biol. Chem. 252, 4790-4795] is discussed.

• Authors: F Nau, G Pham-Coeur-Joly, J M Dubert
• Journal: European journal of biochemistry (Eur J Biochem) Vol. 130 Issue 2 Pg. 261-8 (Feb 01 1983) ISSN: 0014-2956 [Print] England
• PMID: 6825691 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Neoplasm Proteins
• Saccharomyces cerevisiae Proteins
• tRNA Methyltransferases
• NCL1 protein, S cerevisiae
• tRNA(cytosine-5)methyltransferase, mouse
• tRNA (adenine(58)-N(1))-methyltransferase

Topics

• Animals
• Kinetics
• Mice
• Mice, Inbred BALB C
• Molecular Weight
• Neoplasm Proteins (isolation & purification)
• Neoplasms, Experimental (enzymology)
• Plasmacytoma (enzymology)
• Protein Conformation
• Saccharomyces cerevisiae Proteins
• tRNA Methyltransferases (isolation & purification)