2111815

Source:http://linkedlifedata.com/resource/pubmed/id/2111815

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0001480, umls-concept:C0013729, umls-concept:C0441655, umls-concept:C0443199, umls-concept:C1167622, umls-concept:C1709059
pubmed:issue	16
pubmed:dateCreated	1990-7-2
pubmed:abstractText	Eukaryotic initiation factor 2 (eIF-2) is shown to bind ATP with high affinity. Binding of ATP to eIF-2 induces loss of the ability to form a ternary complex with Met-tRNAf and GTP, while still allowing, and even stimulating, the binding of mRNA. Ternary complex formation between eIF-2, GTP, and Met-tRNAf is inhibited effectively by ATP, but not by CTP or UTP. Hydrolysis of ATP is not required for inhibition, for adenyl-5'-yl imidodiphosphate (AMP-PNP), a nonhydrolyzable analogue of ATP, is as active an inhibitor; adenosine 5'-O-(thiotriphosphate) (ATP gamma S) inhibits far more weakly. Ternary complex formation is inhibited effectively by ATP, dATP, or ADP, but not by AMP and adenosine. Hence, the gamma-phosphate of ATP and its 3'-OH group are not required for inhibition, but the beta-phosphate is indispensible. Specific complex formation between ATP and eIF-2 is shown 1) by effective retention of Met-tRNAf- and mRNA-binding activities on ATP-agarose and by the ability of free ATP, but not GTP, CTP, or UTP, to effect elution of eIF-2 from this substrate; 2) by eIF-2-dependent retention of [alpha-32P]ATP or dATP on nitrocellulose filters and its inhibition by excess ATP, but not by GTP, CTP, or UTP. Upon elution from ATP-agarose by high salt concentrations, eIF-2 recovers its ability to form a ternary complex with Met-tRNAf and GTP. ATP-induced inhibition of ternary complex formation is relieved by excess Met-tRNAf, but not by excess GTP or guanyl-5'-yl imidodiphosphate (GMP-PNP). Thus, ATP does not act by inhibiting binding of GTP to eIF-2. Instead, ATP causes Met-tRNAf in ternary complex to dissociate from eIF-2. Conversely, affinity of eIF-2 for ATP is high in the absence of GTP and Met-tRNAf (Kd less than or equal to 10(-12) M), but decreases greatly in conditions of ternary complex formation. These results support the concept that eIF-2 assumes distinct conformations for ternary complex formation and for binding of mRNA, and that these are affected differently by ATP. Interaction of ATP with an eIF-2 molecule in ternary complex with Met-tRNAf and GTP promotes displacement of Met-tRNAf from eIF-2, inducing a state favorable for binding of mRNA. ATP may thus regulate the dual binding activities of eIF-2 during initiation of translation.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/2'-deoxyadenosine triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenylyl Imidodiphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Deoxyadenine Nucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Guanylyl Imidodiphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl, http://linkedlifedata.com/resource/pubmed/chemical/adenosine 5'-O-(3-thiotriphosphate), http://linkedlifedata.com/resource/pubmed/chemical/tRNA(m)(Met), methionine-
pubmed:status	MEDLINE
pubmed:month	Jun
pubmed:issn	0021-9258
pubmed:author	pubmed-author:BanaiYY, pubmed-author:GonskaJJ, pubmed-author:HararyRR, pubmed-author:KaempferRR, pubmed-author:LebendikerM AMA
pubmed:issnType	Print
pubmed:day	5
pubmed:volume	265
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	9083-9
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:2111815-Adenosine Diphosphate, pubmed-meshheading:2111815-Adenosine Triphosphate, pubmed-meshheading:2111815-Adenylyl Imidodiphosphate, pubmed-meshheading:2111815-Animals, pubmed-meshheading:2111815-Binding, Competitive, pubmed-meshheading:2111815-Binding Sites, pubmed-meshheading:2111815-Deoxyadenine Nucleotides, pubmed-meshheading:2111815-Eukaryotic Initiation Factor-2, pubmed-meshheading:2111815-Guanosine Triphosphate, pubmed-meshheading:2111815-Guanylyl Imidodiphosphate, pubmed-meshheading:2111815-Kinetics, pubmed-meshheading:2111815-Macromolecular Substances, pubmed-meshheading:2111815-Penicillium chrysogenum, pubmed-meshheading:2111815-Protein Biosynthesis, pubmed-meshheading:2111815-RNA, Double-Stranded, pubmed-meshheading:2111815-RNA, Messenger, pubmed-meshheading:2111815-RNA, Transfer, Amino Acyl, pubmed-meshheading:2111815-Rabbits
pubmed:year	1990
pubmed:articleTitle	Binding of ATP to eukaryotic initiation factor 2. Differential modulation of mRNA-binding activity and GTP-dependent binding of methionyl-tRNAMetf.
pubmed:affiliation	Department of Molecular Virology, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't