期刊
MOLECULAR CELL
卷 21, 期 1, 页码 87-96出版社
CELL PRESS
DOI: 10.1016/j.molcel.2005.10.036
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资金
- NIGMS NIH HHS [GM52347] Funding Source: Medline
The biological role of many nonessential tRNA modifications outside of the anticodon remains elusive despite their evolutionary conservation. We show here that m(7)G(46) methyltransferase Trm8p/Trm82p acts as a hub of synthetic interactions with several tRNA modification enzymes, resulting in temperature-sensitive growth. Analysis of three double mutants indicates reduced levels of tRNA(Val(AAC)) consistent with a role of the corresponding modifications in maintenance of tRNA levels. Detailed examination of a trm8-Delta trm4-Delta double mutant demonstrates rapid degradation of preexisting tRNA(Val(AAC)) accompanied by its de-amino-acylation. Multiple copies of tRNA(Val(AA)) suppress the trm8-Delta trm4-Delta growth defect, directly implicating this tRNA in the phenotype. These results define a rapid tRNA degradation (RTD) pathway that is independent of the TRF4/RRP6-dependent nuclear surveillance pathway. The degradation of an endogenous tRNA species at a rate typical of mRNA decay demonstrates a critical role of nonessential modifications for tRNA stability and cell survival.
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