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Science 26 May 1989:
Vol. 244. no. 4907, pp. 986 - 989
DOI: 10.1126/science.2471265
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Articles
Science, Vol 244, Issue 4907, 986-989
Copyright © 1989 by American Association for the Advancement of Science
Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine
GR Bjork,
PM Wikstrom,
and
AS Bystrom
Department of Microbiology, Umea University, Sweden.
The methylated nucleoside 1-methylguanosine (m1G) is present next to the 3' end of the anticodon (position 37) in all transfer RNAs (tRNAs) that read codons starting with C except in those tRNAs that read CAN codons. All of the three proline tRNA species, which read CCN codons in Salmonella typhimurium, have been sequenced and shown to contain m1G in position 37. A mutant of S. typhimurium that lacks m1G in its tRNA when grown at temperatures above 37 degrees C, has now been isolated. The mutation (trmD3) responsible for this methylation deficiency is in the structural gene (trmD) for the tRNA(m1G37)methyltransferase. Therefore, the three proline tRNAs in the trmD3 mutant have an unmodified guanosine at position 37. Furthermore, the trmD3 mutation also causes at least one of the tRNAPro species to frequently shift frame when C's are present successively in the message. Thus, m1G appears to prevent frameshifting. The data from eubacteria apply to both eukaryotes and archaebacteria.
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