Transfer RNA methyltransferases from yellow lupin seeds: Purification and properties

H. Wierzbicka, H. Jakubowski, J. Pawelkiewicz

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

tRNA methyltransferases from extract of yellow lupin seeds were purified over 300-fold by the methods based on hydrophobic and affinity chromatography. However, in the most active fractions the methylating enzymes were over 2000 purified. The purified enzyme fractions catalysed the formation of 1-methyladenine and 5-methylcytosine using E. coli B and B. subtilis tRNAs as substrates and Sadenosylmethionine as the methyl donor. They were unable to methylate their own endogenous tRNA but they were capable of methylating tRNA of some other Iupinus species. Whereas the patterns of methylated constituents of tRNA from E.coli and B. subtilis were quite similar, they differed considerably from those obtained with lupin species tRNAs. Some properties of purified methyltransferases from yellow lupin seeds have been described.

Original languageEnglish (US)
Pages (from-to)101-112
Number of pages12
JournalNucleic acids research
Volume2
Issue number1
DOIs
StatePublished - Jan 1975

All Science Journal Classification (ASJC) codes

  • Genetics

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