Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2009-5-7
pubmed:databankReference
pubmed:abstractText
Post-transcriptional RNA modifications in the anticodon of transfer RNAs frequently contribute to the high fidelity of protein synthesis. In eubacteria, two genome-encoded transfer RNA (tRNA) species bear the same CAU sequence as the anticodons, which are differentiated by modified cytidines at the wobble positions. The elongator tRNA(Met) accepts an acetyl moiety at the wobble base to form N(4)-acetylcytidine (ac(4)C): an inherent modification ensures precise decoding of the AUG codon by strengthening C-G base-pair interaction and concurrently preventing misreading of the near cognate AUA codon. We have determined the crystal structure of tRNA(Met) cytidine acetyltransferase (TmcA) from Escherichia coli complexed with two natural ligands, acetyl-CoA and ADP, at 2.35 A resolution. The structure unexpectedly reveals an idiosyncratic RNA helicase module fused with a GCN5-related N-acetyltransferase (GNAT) fold, which intimately cross-interact. Taken together with the biochemical evidence, we further unravelled the function of acetyl-CoA as an enzyme-activating switch, and propose that an RNA helicase motor driven by ATP hydrolysis is used to deliver the wobble base to the active centre of the GNAT domain.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-10376676, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-10485713, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-10777508, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-10811654, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-11087862, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-11171974, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-11278350, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-11545728, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-11720294, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-11779468, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-11839499, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-1378397, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-14527414, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-15028736, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-15581578, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-15585580, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16039592, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16337753, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16387657, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16415880, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16421450, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16630817, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16700561, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16809541, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16871210, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-16923391, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-17159905, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-17187822, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-18668122, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-2608479, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-3054566, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-3132458, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-355249, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-8385989, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-8568876, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-9204872, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-9219684, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-9399834, http://linkedlifedata.com/resource/pubmed/commentcorrection/19322199-9493270
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1460-2075
pubmed:author
pubmed:issnType
Electronic
pubmed:day
6
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1362-73
pubmed:dateRevised
2010-9-23
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon.
pubmed:affiliation
Faculty of Advanced Life Sciences, Hokkaido University, Sapporo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't