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Titolo:
Repressor binding to a dorsal regulatory site traps human elF4E in a high cap-affinity state
Autore:
Ptushkina, M; von der Haar, T; Karim, MM; Hughes, JMX; McCarthy, JEG;
Indirizzi:
UMIST, Dept Biomol Sci, Posttranscript Control Grp, Manchester M60 1QD, Lancs, England UMIST Manchester Lancs England M60 1QD Manchester M60 1QD, Lancs, England
Titolo Testata:
EMBO JOURNAL
fascicolo: 14, volume: 18, anno: 1999,
pagine: 4068 - 4075
SICI:
0261-4189(19990715)18:14<4068:RBTADR>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
5'-CAP-BINDING PROTEIN EIF4E; TRANSLATION FACTOR EIF4E; MESSENGER-RNA 5'-CAP; SACCHAROMYCES-CEREVISIAE; DEPENDENT TRANSLATION; PHOSPHORYLATION SITES; INITIATION FACTOR-4E; GENE-EXPRESSION; CELL-GROWTH; YEAST;
Keywords:
cap-binding affinity; eIF4E dorsal binding site; eukaryotic translation initiation factors 4E and 4G; gene expression; regulation by 4E-binding proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: McCarthy, JEG UMIST, Dept Biomol Sci, Posttranscript Control Grp, POB 88, Manchester M601QD, Lancs, England UMIST POB 88 Manchester Lancs England M601QD Lancs, England
Citazione:
M. Ptushkina et al., "Repressor binding to a dorsal regulatory site traps human elF4E in a high cap-affinity state", EMBO J, 18(14), 1999, pp. 4068-4075

Abstract

Eukaryotic translation initiation involves recognition of the 5' end of cellular mRNA by the cap-binding complex known as eukaryotic initiation factor 4F (eIF4F), Initiation is a key point of regulation in gene expression inresponse to mechanisms mediated by signal transduction pathways. We have investigated the molecular interactions underlying inhibition of human eIF4Efunction by regulatable repressors called 4E-binding proteins (4E-BPs), Two essential components of eIF4F are the cap-binding protein eIF4E, and eIF4G, a multi-functional protein that binds both eIF4E and other essential eIFs, We show that the 4E-BPs 1 and 2 block the interaction between eIF4G and eIF4E by competing for binding to a dorsal site on eIF4E, Remarkably, binding of the 4E-BPs at this dorsal site enhances cap-binding via the ventral cap-binding slot, thus trapping eIF4E in inactive complexes with high affinity for capped mRNA, The binding contacts and affinities for the interactions between 4E-BP1/2 and eIF4E are distinct (estimated K-d values of 10(-8) and 3 x 10(-9) for 4E-BP1 and 2, respectively), and the differences in theseproperties are determined by three amino acids within an otherwise conserved motif, These data provide a quantitative framework for a new molecular model of translational regulation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 22:44:14