Isolation and characterization of a tRNA(guanine-7-)-methyltransferase from Salmonella typhimurium.

Abstract:

:The tRNA modifying enzyme, S-adenosylmethionine:tRNA(guanine-7-)-methyltransferase, has been extensively purified from Salmonella typhimurium. A rapid and efficient purification method using phosphocellulose chromatography followed by ammonium sulfate precipitation and Sephadex G-100 gel filtration is described. The enzyme appears to be a single polypeptide chain with a molecular weight of approximately 25 000--30 000 daltons. The Km for S-adenosylmethionine and for undermethylated tRNA is 53 microM and 3.4 microM, respectively. The methylation reaction is dependent on added monovalent or divalent cations; 5 mM spermidine, 3 mM MgCl2 and 1 mM spermine are the most effective. The enzyme, though not homogeneous, is free from contaminating ribonucleases and other tRNA methyltransferases.

journal_name

Mol Cell Biochem

authors

Colonna A,Ciliberto G,Santamaria R,Cimino F,Salvatore F

doi

10.1007/BF00224919

subject

Has Abstract

pub_date

1983-01-01 00:00:00

pages

97-106

issue

2

eissn

0300-8177

issn

1573-4919

journal_volume

52

pub_type

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