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rdf:type |
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lifeskim:mentions |
umls-concept:C0033414,
umls-concept:C0036576,
umls-concept:C0070348,
umls-concept:C0242610,
umls-concept:C0439855,
umls-concept:C0752615,
umls-concept:C0851285,
umls-concept:C1136317,
umls-concept:C1412810,
umls-concept:C1414323,
umls-concept:C1414359,
umls-concept:C1417607,
umls-concept:C1423773,
umls-concept:C1704675,
umls-concept:C1706853,
umls-concept:C1711351,
umls-concept:C1879748
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pubmed:issue |
21
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pubmed:dateCreated |
2004-10-15
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pubmed:abstractText |
The N-terminal domain (NTD) of NIP1/eIF3c interacts directly with eIF1 and eIF5 and indirectly through eIF5 with the eIF2-GTP-Met-tRNA(i)(Met) ternary complex (TC) to form the multifactor complex (MFC). We investigated the physiological importance of these interactions by mutating 16 segments spanning the NIP1-NTD. Mutations in multiple segments reduced the binding of eIF1 or eIF5 to the NIP1-NTD. Mutating a C-terminal segment of the NIP1-NTD increased utilization of UUG start codons (Sui(-) phenotype) and was lethal in cells expressing eIF5-G31R that is hyperactive in stimulating GTP hydrolysis by the TC at AUG codons. Both effects of this NIP1 mutation were suppressed by eIF1 overexpression, as was the Sui(-) phenotype conferred by eIF5-G31R. Mutations in two N-terminal segments of the NIP1-NTD suppressed the Sui(-) phenotypes produced by the eIF1-D83G and eIF5-G31R mutations. From these and other findings, we propose that the NIP1-NTD coordinates an interaction between eIF1 and eIF5 that inhibits GTP hydrolysis at non-AUG codons. Two NIP1-NTD mutations were found to derepress GCN4 translation in a manner suppressed by overexpressing the TC, indicating that MFC formation stimulates TC recruitment to 40S ribosomes. Thus, the NIP1-NTD is required for efficient assembly of preinitiation complexes and also regulates the selection of AUG start codons in vivo.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-10075937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-10228174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-10659855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-11018020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-11331597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12008673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12411506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12435632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12471154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12493757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12514125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12651896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12860115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-12861028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-1332047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-14600024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-14976554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-1729602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-2017175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-3043201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-3073106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-3474623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-3516411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-7876188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-9308967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-9671501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15485912-9732867
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Codon, Initiator,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-1,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-3,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-5,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/NIP1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Prokaryotic Initiation Factor-3,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Met,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9437-55
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15485912-Alanine,
pubmed-meshheading:15485912-Saccharomyces cerevisiae,
pubmed-meshheading:15485912-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15485912-Models, Molecular,
pubmed-meshheading:15485912-Protein Structure, Quaternary,
pubmed-meshheading:15485912-Protein Subunits,
pubmed-meshheading:15485912-Protein Biosynthesis,
pubmed-meshheading:15485912-Ribosomes,
pubmed-meshheading:15485912-Amino Acid Sequence,
pubmed-meshheading:15485912-Protein Binding,
pubmed-meshheading:15485912-Phenotype,
pubmed-meshheading:15485912-Molecular Sequence Data,
pubmed-meshheading:15485912-Guanosine Triphosphate,
pubmed-meshheading:15485912-Nuclear Proteins,
pubmed-meshheading:15485912-RNA, Transfer, Met,
pubmed-meshheading:15485912-Protein Kinases,
pubmed-meshheading:15485912-DNA-Binding Proteins,
pubmed-meshheading:15485912-Codon, Initiator,
pubmed-meshheading:15485912-Prokaryotic Initiation Factor-3,
pubmed-meshheading:15485912-Eukaryotic Initiation Factor-3,
pubmed-meshheading:15485912-Gene Expression Regulation, Fungal
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