Linked Life Data

2322578

Source:http://linkedlifedata.com/resource/pubmed/id/2322578

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pubmed-article:2322578pubmed:abstractTextThe accessibility of three amino acids of EF-2, located within highly conserved regions near the N- and C-terminal extremities of the molecule (the E region and the ADPR region, respectively) to modifying enzymes has been compared within nucleotide-complexed EF-2 and ribosomal complexes that mimic the pre- and posttranslocational ones: the high-affinity complex (EF-2)-nonhydrolysable GTP analog GuoPP[CH2]P ribosome and the low-affinity (EF-2)-GDP-ribosome complex, EF-2 and ribosomes being from rat liver. We studied the reactivity of two highly conserved residues diphthamide-715 and Arg-66, to diphtheria-toxin-dependent ADP-ribosylation and trypsin attack, and of a threonine that probably lies between residues 51 and 60, to phosphorylation by a Ca2+/calmodulin-dependent protein kinase. Diphthamide 715 and this threonine residue were unreactive within the high-affinity complex but seemed fully reactive in the low-affinity complex. Arg-66 was resistant to trypsin in both complexes. The possible involvement of the E and ADPR regions of EF-2 in the interaction with ribosome in the two complexes is discussed.lld:pubmed
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pubmed-article:2322578pubmed:authorpubmed-author:ReboudJ PJPlld:pubmed
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pubmed-article:2322578pubmed:pagination231-7lld:pubmed
pubmed-article:2322578pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:2322578pubmed:articleTitleModification of the reactivity of three amino-acid residues in elongation factor 2 during its binding to ribosomes and translocation.lld:pubmed
pubmed-article:2322578pubmed:affiliationLaboratoire de Biochimie Médicale, Université Claude Bernard, Villeurbanne, France.lld:pubmed
pubmed-article:2322578pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2322578pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed