PMID:8419334
| Citation |
Gustafsson, C and Björk, GR (1993) The tRNA-(m5U54)-methyltransferase of Escherichia coli is present in two forms in vivo, one of which is present as bound to tRNA and to a 3'-end fragment of 16 S rRNA. J. Biol. Chem. 268:1326-31 |
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| Abstract |
The enzyme tRNA-(m5U54)-methyltransferase (EC 2.1.1.35) of Escherichia coli catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to uridine in position 54 of the T psi-loop of all E. coli tRNA species, forming 5-methyluridine (m5U). In vivo, this enzyme is present both as a native polypeptide of 42 kDa and as a TrmA.RNA complex. The TrmA.RNA complex is not dissociated during strong denaturing conditions such as boiling in 8 M urea or 6 M guanidine HCl, consisting with that the RNA is covalently bound to the protein. After sequencing and Southern blot analyses, the RNA was identified to be a subset of undermodified tRNA species as well as the 3' terminus of 16 S rRNA. However, the complex is not associated with the ribosome and the covalently bound RNA does not affect the tRNA methylating activity of the enzyme. |
| Links | |
| Keywords |
Base Sequence; Binding Sites; Blotting, Western; Centrifugation, Density Gradient; Chromatography, Ion Exchange; Escherichia coli/enzymology; Escherichia coli/genetics; Kinetics; Models, Structural; Molecular Sequence Data; Nucleic Acid Conformation; Operon; Protein Binding; RNA, Ribosomal, 16S/chemistry; RNA, Ribosomal, 16S/isolation & purification; RNA, Ribosomal, 16S/metabolism; RNA, Transfer/metabolism; S-Adenosylmethionine/pharmacology; tRNA Methyltransferases/isolation & purification; tRNA Methyltransferases/metabolism |
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