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Stringent regulation of the synthesis of a transfer ribonucleic acid biosynthetic enzyme: transfer ribonucleic acid(m5U)methyltransferase from Escherichia coli.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
1977 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 130, no 2, 635-41 p.Article in journal (Refereed) Published
Abstract [en]

This paper describes the regulation of a transfer ribonucleic acid (tRNA) biosynthetic enzyme, the tRNA(m5U)methyltransferase (EC 2.1.1.35). This enzyme catalyzes the formation of 5-methyluridine (m5U, ribothymidine) in all tRNA chains of Escherichia coli. Partial deprivation of charged tRNAVal can be imposed by shifting strains carrying a temperature-sensitive valyl-tRNA ligase from a permissive to a semipermissive temperature. By using two such strains differing only in the allelic state of the relA gene, it was possible to show the tRNA(m5U)methyltransferase to be stringently regulated. Upon partial deprivation of charged tRNAVal, the differential rate of tRNA(m5U)methyltransferase synthesis was found to decrease in a strain with stringent RNA control (relA+), whereas it increased in the strain carrying the relA allele. This increase of accumulation of tRNA(m5U)methyltransferase activity required protein synthesis. Thus, when tRNA is partially uncharged in the cell, the relA gene product influences the expression of tRNA(m5U)methyltransferase gene.

Place, publisher, year, edition, pages
1977. Vol. 130, no 2, 635-41 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:umu:diva-59748PubMedID: 95660OAI: oai:DiVA.org:umu-59748DiVA: diva2:556405
Available from: 2012-09-25 Created: 2012-09-25 Last updated: 2017-12-07

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