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rdf:type |
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lifeskim:mentions |
umls-concept:C0013729,
umls-concept:C0018353,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0034493,
umls-concept:C0035286,
umls-concept:C0439855,
umls-concept:C0597295,
umls-concept:C1521761,
umls-concept:C1521970,
umls-concept:C1522492,
umls-concept:C1550101,
umls-concept:C1555029,
umls-concept:C1881488,
umls-concept:C1999216
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pubmed:issue |
11
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pubmed:dateCreated |
1980-3-17
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pubmed:abstractText |
During heme deficiency in reticulocyte lysates, a translational inhibitor (heme-regulated inhibitor, HRI) that blocks polypeptide chain initiation is activated. HRI is a protein kinase that specifically phosphorylates the 38,000-dalton subunit of the Met-tRNAfMet binding factor, eIF-2. Phosphorylation of eIF-2 by HRI prevents its interaction with at least two additional factors, resulting in a net reduction in formation of ternary complex (Met-tRNAfMet.eIF-2.GTP) and AUG-dependent transfer of Met-tRNAfMet to 40S ribosomal subunits. A factor (sRF) that reverses protein synthesis inhibition in heme-deficient lysates has been purified from reticulocyte postribosomal supernatant. sRF also reverses the inhibition of ternary complex formation by HRI in a fractionated system. The ternary complex inhibition reversal activity and the protein synthesis inhibition reversal activity cosediment at 12.5 S upon glycerol density gradient centrifugation, and both activities are sensitive to heat or N-ethylmaleimide. Purified sRF does not dephosphorylate eIF-2 whose phosphorylation has been catalyzed by HRI, nor does the sRF prevent the phosphorylation of eIF-2 by HRI in a fractionated system. sRF stimulates ternary complex formation by both phosphorylated and nonphosphorylated eIF-2. These observations suggest that the sensitivity of protein synthesis to phosphorylation of eIF-2 by HRI may be modulated by the concentration and activity of sRF.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-1066685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-1069987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-1201099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-14282023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-184458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-184460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-220606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-249314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-272639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-273238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-275839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-278981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-283396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-286294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-291924,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-323054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-4512619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-4528641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-459901,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-4762417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-5037023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-5221248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-5238986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-5266178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-5488930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-559547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-5656815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-592398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-655375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-836310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-907668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-921787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-942051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-947756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-971309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-974137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293657-977577
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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 |
Nov
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
76
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5490-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:293657-Animals,
pubmed-meshheading:293657-Cytosol,
pubmed-meshheading:293657-Guanosine Triphosphate,
pubmed-meshheading:293657-Heme,
pubmed-meshheading:293657-Methionine,
pubmed-meshheading:293657-Molecular Weight,
pubmed-meshheading:293657-Peptide Chain Initiation, Translational,
pubmed-meshheading:293657-Peptide Initiation Factors,
pubmed-meshheading:293657-Phosphorylation,
pubmed-meshheading:293657-Protein Binding,
pubmed-meshheading:293657-RNA, Transfer, Amino Acyl,
pubmed-meshheading:293657-Rabbits,
pubmed-meshheading:293657-Reticulocytes
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pubmed:year |
1979
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pubmed:articleTitle |
Protein synthesis in rabbit reticulocytes: characteristics of a postribosomal supernatant factor that reverses inhibition of protein synthesis in heme-deficient lysates and inhibition of ternary complex (Met-tRNAfMet.eIF-2.GTP) formation by heme-regulated inhibitor.
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pubmed:publicationType |
Journal Article
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