Document Detail


Rapid tRNA decay can result from lack of nonessential modifications.
MedLine Citation:
PMID:  16387656     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The biological role of many nonessential tRNA modifications outside of the anticodon remains elusive despite their evolutionary conservation. We show here that m7G46 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-aminoacylation. Multiple copies of tRNA(Val(AAC)) 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.
Authors:
Andrei Alexandrov; Irina Chernyakov; Weifeng Gu; Shawna L Hiley; Timothy R Hughes; Elizabeth J Grayhack; Eric M Phizicky
Related Documents :
8347586 - A new function of s-adenosylmethionine: the ribosyl moiety of adomet is the precursor o...
3882706 - Transfer rna splicing in saccharomyces cerevisiae. secondary and tertiary structures of...
21309606 - Self-assembly of short aβ(16-22) peptides: effect of terminal capping and the role of e...
9440046 - X-ray structures of aza-proline-containing peptides.
6173096 - Regional distribution of alpha- and gamma-type endorphins in rat brain.
22916716 - Self-assembly of highly ordered peptide amphiphile metallo-porphyrin arrays.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular cell     Volume:  21     ISSN:  1097-2765     ISO Abbreviation:  Mol. Cell     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2006-01-02     Completed Date:  2006-02-27     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  87-96     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Biophysics, University of Rochester School of Medicine, Rochester, New York 14642, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Anticodon
Gene Deletion
Humans
Nucleic Acid Conformation
Oligonucleotide Array Sequence Analysis
RNA Processing, Post-Transcriptional*
RNA Stability*
RNA, Transfer, Val / genetics,  metabolism*
Saccharomyces cerevisiae / cytology,  physiology
Saccharomyces cerevisiae Proteins / genetics,  metabolism
Temperature
Transfer RNA Aminoacylation
tRNA Methyltransferases / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
GM52347/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Anticodon; 0/RNA, Transfer, Val; 0/Saccharomyces cerevisiae Proteins; EC 2.1.1.-/tRNA Methyltransferases; EC 2.1.1.33/tRNA (guanine-N7-)-methyltransferase
Comments/Corrections
Comment In:
Mol Cell. 2006 Jan 20;21(2):144-5   [PMID:  16427003 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase II...
Next Document:  Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynth...