| pubmed-article:6591195 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C1524059 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C0031327 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C0035286 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C0597295 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C1555029 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C1514566 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:6591195 | lifeskim:mentions | umls-concept:C1881488 | lld:lifeskim |
| pubmed-article:6591195 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:6591195 | pubmed:dateCreated | 1984-10-24 | lld:pubmed |
| pubmed-article:6591195 | pubmed:abstractText | A eukaryotic initiation factor 2 (eIF-2)-ancillary protein factor Co-eIF-2 promotes displacement of GDP from eIF-2 X GDP and facilitates ternary complex (Met-tRNAf X eIF-2 X GTP) formation in the presence of Mg2+. Heme-regulated protein synthesis inhibitor, HRI, phosphorylates the alpha-subunit of eIF-2 and thus inhibits ternary complex formation as Co-eIF-2 does not displace GDP from eIF-2 alpha (P) X GDP. RF, a high molecular weight cell supernatant factor, reverses protein synthesis inhibition in heme-deficient reticulocyte lysates and also reverses HRI inhibition of ternary complex formation. RF contains Co-eIF-2 activity. In addition, an active RF preparation contains excess alpha-subunit of eIF-2 in the free and unphosphorylated form and this alpha-subunit of eIF-2 is not phosphorylated by HRI and ATP. In this paper we report (i) an active RF preparation contains excess alpha-subunit of eIF-2 and this alpha-subunit can be phosphorylated by HRI and ATP in the presence of GDP; (ii) RF promotes ternary complex formation by eIF-2 X [3H]GDP with accompanying GDP displacement; (iii) in the presence of HRI and ATP, RF promotes ternary complex formation by eIF-2 X [3H]GDP without accompanying GDP displacement; (iv) in the presence of HRI and ATP, the ternary complex formed using RF is active in Met-tRNAf X 40S initiation complex formation; (v) both the ternary complex and the Met-tRNAf X 40S complex formation in the presence of HRI and ATP are completely inhibited by prior incubation of RF with GDP; (vi) upon further fractionation of an active RF fraction, a preparation can be obtained that contains HRI-sensitive Co-eIF-2 activity. However, this preparation does not efficiently reverse protein synthesis inhibition in heme-deficient reticulocyte lysates and does not contain excess alpha-subunit of eIF-2. Based on these observations, we have suggested (a) RF provides the unphosphorylated alpha-subunit to eIF-2 alpha (P) X GDP and restores eIF-2 activity. This RF activity is inhibited as the alpha-subunit in the RF preparation becomes phosphorylated by HRI and ATP in the presence of GDP; (b) RF contains Co-eIF-2 activity, which has dual functions: (i) stimulation of ternary complex formation by eIF-2 and (ii) GDP displacement from eIF-2 X GDP during ternary complex formation. In the presence of HRI and ATP, Co-eIF-2 but does not displace GDP from eIF-2 alpha(P) X GDP. | lld:pubmed |
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| pubmed-article:6591195 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6591195 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6591195 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6591195 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6591195 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6591195 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6591195 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:6591195 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:OlsonCC | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:AhmadFF | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:BanerjeeAA | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:BagchiMM | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:GraceMM | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:GuptaN KNK | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:ChakravartyII | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:NasrinNN | lld:pubmed |
| pubmed-article:6591195 | pubmed:author | pubmed-author:YeagerTT | lld:pubmed |
| pubmed-article:6591195 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6591195 | pubmed:volume | 81 | lld:pubmed |
| pubmed-article:6591195 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6591195 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6591195 | pubmed:pagination | 5379-83 | lld:pubmed |
| pubmed-article:6591195 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:6591195 | pubmed:meshHeading | pubmed-meshheading:6591195-... | lld:pubmed |
| pubmed-article:6591195 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6591195 | pubmed:articleTitle | Protein synthesis in rabbit reticulocytes: a study of the mechanism of action of the protein factor RF that reverses protein synthesis inhibition in heme-deficient reticulocyte lysates. | lld:pubmed |
| pubmed-article:6591195 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6591195 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6591195 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6591195 | lld:pubmed |
