Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
2008-10-27
pubmed:abstractText
Selection of the AUG start codon for translation in eukaryotes is governed by codon-anticodon interactions between the initiator Met-tRNA(i)(Met) and the mRNA. Translation initiation factor 2 (eIF2) binds Met-tRNA(i)(Met) to the 40S ribosomal subunit, and previous studies identified Sui(-) mutations in eIF2 that enhanced initiation from a noncanonical UUG codon, presumably by impairing Met-tRNA(i)(Met) binding. Consistently, an eIF2gamma-N135D GTP-binding domain mutation impairs Met-tRNA(i)(Met) binding and causes a Sui(-) phenotype. Intragenic A208V and A382V suppressor mutations restore Met-tRNA(i)(Met) binding affinity and cell growth; however, only A208V suppresses the Sui(-) phenotype associated with the eIF2gamma-N135D mutation. An eIF2gamma-A219T mutation impairs Met-tRNA(i)(Met) binding but unexpectedly enhances the fidelity of initiation, suppressing the Sui(-) phenotype associated with the eIF2gamma-N135D,A382V mutant. Overexpression of eIF1, which is thought to monitor codon-anticodon interactions during translation initiation, likewise suppresses the Sui(-) phenotype of the eIF2gamma mutants. We propose that structural alterations in eIF2gamma subtly alter the conformation of Met-tRNA(i)(Met) on the 40S subunit and thereby affect the fidelity of start codon recognition independent of Met-tRNA(i)(Met) binding affinity.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-11701921, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-11927566, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-12861028, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-14600024, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-14688270, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-14698289, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-15485912, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-15601822, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-15664195, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-16153175, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-16246727, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-16522633, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-17189426, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-1729602, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-17434125, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-17504939, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-18000047, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-2017175, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-2179049, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-2649894, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-2678106, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-3136928, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-6354131, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-7491491, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-7774582, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-8939739, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-8947054, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-9242920, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-9308967, http://linkedlifedata.com/resource/pubmed/commentcorrection/18794367-9732867
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1098-5549
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6877-88
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18794367-Amino Acid Sequence, pubmed-meshheading:18794367-Basic-Leucine Zipper Transcription Factors, pubmed-meshheading:18794367-Codon, Initiator, pubmed-meshheading:18794367-DNA-Binding Proteins, pubmed-meshheading:18794367-Eukaryotic Initiation Factor-2, pubmed-meshheading:18794367-Models, Molecular, pubmed-meshheading:18794367-Molecular Sequence Data, pubmed-meshheading:18794367-Mutation, pubmed-meshheading:18794367-Nucleic Acid Conformation, pubmed-meshheading:18794367-Phenotype, pubmed-meshheading:18794367-Protein Structure, Tertiary, pubmed-meshheading:18794367-RNA, Transfer, Met, pubmed-meshheading:18794367-Saccharomyces cerevisiae, pubmed-meshheading:18794367-Saccharomyces cerevisiae Proteins, pubmed-meshheading:18794367-Sequence Alignment, pubmed-meshheading:18794367-Transcription Factors
pubmed:year
2008
pubmed:articleTitle
Translation initiation factor 2gamma mutant alters start codon selection independent of Met-tRNA binding.
pubmed:affiliation
Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Intramural