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Fragmented E. coli methionine tRNA f as methyl acceptor for rat liver tRNA methylase: alteration of the site of methylation by the conformational change of tRNA structure resulting from fragmentation
- Source :
- Biochemical and biophysical research communications. 43(3)
- Publication Year :
- 1971
-
Abstract
- In vitro methylation of E. coli tRNAfMet fragments or their reconstituted molecule by rat liver methylase showed that (1) the whole tRNA molecule was not necessary for recognition by tRNA methylase, and (2) the extent and the site of methylation of fragments differed depending upon the type of fragment used. This indicates that the conformational structure of the methyl acceptor molecule is important for recognition by the tRNA methylase.
- Subjects :
- Electrophoresis
Paper
Conformational change
S-Adenosylmethionine
Methyltransferase
Guanine
Chemical Phenomena
Formates
Polynucleotides
Biophysics
Biology
Biochemistry
Methylation
chemistry.chemical_compound
Methionine
Ribonucleases
RNA, Transfer
Transferases
Escherichia coli
Animals
Fragmentation (cell biology)
Molecular Biology
Pancreas
Carbon Isotopes
Binding Sites
Nucleosides
Cell Biology
Methyltransferases
Alkaline Phosphatase
Chromatography, Ion Exchange
Acceptor
Nucleotidyltransferases
In vitro
Rats
Chemistry
RNA, Bacterial
chemistry
Liver
Transfer RNA
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 43
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....26b85b89f9a057991a47700f1f8df747