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Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine

Björk, Glenn R (author)
Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)
Wikström, P M (author)
Byström, Anders S (author)
Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)
 (creator_code:org_t)
1989
1989
English.
In: Science. - 0036-8075 .- 1095-9203. ; 244:4907, s. 986-989
  • Journal article (peer-reviewed)
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  • 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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