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rdf:type |
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lifeskim:mentions |
umls-concept:C0013729,
umls-concept:C0033414,
umls-concept:C0086597,
umls-concept:C0271510,
umls-concept:C0439855,
umls-concept:C0752615,
umls-concept:C1167622,
umls-concept:C1414323,
umls-concept:C1429001,
umls-concept:C1514562,
umls-concept:C1515655,
umls-concept:C1539339,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
2
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pubmed:dateCreated |
2003-1-6
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pubmed:abstractText |
Translation initiation factor 1A (eIF1A) is predicted to bind in the decoding site of the 40S ribosome and has been implicated in recruitment of the eIF2-GTP-Met-tRNA i Met ternary complex (TC) and ribosomal scanning. We show that the unstructured C-terminus of eIF1A interacts with the C-terminus of eIF5B, a factor that stimulates 40S-60S subunit joining, and removal of this domain of eIF1A diminishes translation initiation in vivo. These findings support the idea that eIF1A-eIF5B association is instrumental in releasing eIF1A from the ribosome after subunit joining. A larger C-terminal truncation that removes a 3(10) helix in eIF1A deregulates GCN4 translation in a manner suppressed by overexpressing TC, implicating eIF1A in TC binding to 40S ribosomes in vivo. The unstructured N-terminus of eIF1A interacts with eIF2 and eIF3 and is required at low temperatures for a step following TC recruitment. We propose a modular organization for eIF1A wherein a core ribosome-binding domain is flanked by flexible segments that mediate interactions with other factors involved in recruitment of TC and release of eIF1A at subunit joining.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10037688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10075937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10200264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10428486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10619838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10659855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10678173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-10982835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-11018020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-11114334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-11228145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-11331597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-11506895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-12008673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-1739968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-2017175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-2038326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-2200518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-3073106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-3323810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-4569079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-6310324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-6336730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-7565788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-7739034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-8242751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-8368005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-8642589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-9135158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-9199350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-9624054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12514125-9671501
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
193-204
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12514125-Binding Sites,
pubmed-meshheading:12514125-Eukaryotic Initiation Factor-1,
pubmed-meshheading:12514125-Eukaryotic Initiation Factor-2,
pubmed-meshheading:12514125-Eukaryotic Initiation Factor-3,
pubmed-meshheading:12514125-Eukaryotic Initiation Factor-5,
pubmed-meshheading:12514125-Macromolecular Substances,
pubmed-meshheading:12514125-Peptide Chain Initiation, Translational,
pubmed-meshheading:12514125-Peptide Initiation Factors,
pubmed-meshheading:12514125-Phenotype,
pubmed-meshheading:12514125-Protein Binding,
pubmed-meshheading:12514125-Protein Biosynthesis,
pubmed-meshheading:12514125-Protein Conformation,
pubmed-meshheading:12514125-Recombinant Fusion Proteins,
pubmed-meshheading:12514125-Ribosomes,
pubmed-meshheading:12514125-Saccharomyces cerevisiae,
pubmed-meshheading:12514125-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12514125-Two-Hybrid System Techniques
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pubmed:year |
2003
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pubmed:articleTitle |
Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo.
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pubmed:affiliation |
Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA.
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