Linked Life Data

8144499

Source:http://linkedlifedata.com/resource/pubmed/id/8144499

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1994-5-5
pubmed:abstractText
The acceptor helix of histidine tRNAs in Escherichia coli is capped by a unique base pair in which the cytosine at the discriminator position is paired with an extra guanosine at -1. In previous in vitro studies, the presence of the G-1:C73 base pair was found to be required to obtain both optimal histidylation by histidyl-tRNA synthetase and accurate 5' processing by RNase P. We investigated the role of G-1:C73 in histidine tRNA identity and found that nucleotide substitutions conferred mischarging by other amino acids in a pattern that correlated with the discriminator base and not with the extra nucleotide at -1. As shown by primer extension experiments, the relatively minor role of the -1 nucleotide in vivo could be attributed to altered RNase P processing. These studies show that interactions of tRNAs in vivo both with RNase P during tRNA biosynthesis and with the pool of aminoacyl-tRNA synthetases can modulate the effects of substitutions at recognition nucleotides, eliciting changes in transfer RNA identity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10022-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Cytosine 73 is a discriminator nucleotide in vivo for histidyl-tRNA in Escherichia coli.
pubmed:affiliation
Department of Biochemistry, University of Vermont College of Medicine, Burlington 05405.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.