| pubmed-article:11101534 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C0035553 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1415018 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1426334 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C0443299 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11101534 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:11101534 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:11101534 | pubmed:dateCreated | 2000-12-26 | lld:pubmed |
| pubmed-article:11101534 | pubmed:abstractText | GCN2 stimulates GCN4 translation in amino acid-starved cells by phosphorylating the alpha-subunit of translation initiation factor 2. GCN2 function in vivo requires the GCN1/GCN20 complex, which binds to the N-terminal domain of GCN2. A C-terminal segment of GCN1 (residues 2052-2428) was found to be necessary and sufficient for binding GCN2 in vivo and in vitro. Overexpression of this fragment in wild-type cells impaired association of GCN2 with native GCN1 and had a dominant Gcn(-) phenotype, dependent on Arg2259 in the GCN1 fragment. Substitution of Arg2259 with Ala in full-length GCN1 abolished complex formation with native GCN2 and destroyed GCN1 regulatory function. Consistently, the Gcn(-) phenotype of gcn1-R2259A, but not that of gcn1Delta, was suppressed by overexpressing GCN2. These findings prove that GCN2 binding to the C-terminal domain of GCN1, dependent on Arg2259, is required for high level GCN2 function in vivo. GCN1 expression conferred sensitivity to paromomycin in a manner dependent on its ribosome binding domain, supporting the idea that GCN1 binds near the ribosomal acceptor site to promote GCN2 activation by uncharged tRNA. | lld:pubmed |
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| pubmed-article:11101534 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11101534 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11101534 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11101534 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11101534 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11101534 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11101534 | pubmed:author | pubmed-author:HinnebuschA... | lld:pubmed |
| pubmed-article:11101534 | pubmed:author | pubmed-author:SattleggerEE | lld:pubmed |
| pubmed-article:11101534 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11101534 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11101534 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:11101534 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11101534 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11101534 | pubmed:pagination | 6622-33 | lld:pubmed |
| pubmed-article:11101534 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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