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Titolo:
A second eIF4E protein in Schizosaccharomyces pombe has distinct eIF4G-binding properties
Autore:
Ptushkina, M; Berthelot, K; von der Haar, T; Geffers, L; Warwicker, J; McCarthy, JEG;
Indirizzi:
Univ Manchester, Inst Sci & Technol, Dept Biomol Sci, Posttranscript Control Grp, Manchester M60 1QD, Lancs, England Univ Manchester Manchester Lancs England M60 1QD M60 1QD, Lancs, England
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 22, volume: 29, anno: 2001,
pagine: 4561 - 4569
SICI:
0305-1048(20011115)29:22<4561:ASEPIS>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CAP-BINDING PROTEIN; INITIATION-FACTOR EIF-4E; DEPENDENT TRANSLATION INITIATION; MESSENGER-RNA 5'-CAP; FACTOR 4G EIF4G; SACCHAROMYCES-CEREVISIAE; CAENORHABDITIS-ELEGANS; YEAST; CELL; STABILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: McCarthy, JEG Univ Manchester, Inst Sci & Technol, Dept Biomol Sci, Posttranscript Control Grp, Manchester M60 1QD, Lancs, England Univ Manchester Manchester Lancs England M60 1QD s, England
Citazione:
M. Ptushkina et al., "A second eIF4E protein in Schizosaccharomyces pombe has distinct eIF4G-binding properties", NUCL ACID R, 29(22), 2001, pp. 4561-4569

Abstract

The eukaryotic cap-binding proteins belonging to the! eIF4E family are generally involved in mediating the: recruitment of ribosomes to capped mRNA. We described previously a cap-binding protein (now, called eIF4E1) in Schizosaccharomyces pombe that appears to have all of the usual structural and functional attributes of an eIF4E. We have now characterised a new type of cap-binding protein (eIF4E2) from this organism, which at the amino acid sequence level, is 52% identical and 59% similar to eIF4E1. eIF4E2 is not essential in S.pombe but has some: novel properties that may be related to a special function in the cell. The ratio of eIF4E2:eIF4E1 in the: cell shifts in favour of eIF4E2 at higher temperatures. Despite having all of the dorsal face amino acids that have so far been associated with eIF4G binding to eIF4E1, eIF4E2 binds the eIF4E-binding domain of S.pombe eIF4G >10(2)-times weaker than eIF4E1 in vitro. The eIF4E2 cap-binding affinity is in the: typical micromolar range. The results suggest that eIF4E2 is not active on themain pathway, of translation initiation in fission yeast but might play a role in the adaptation strategy of this organism under specific growth conditions. Moreover, they prov ide insight into the molecular characteristics required for tight binding to eIF4G.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 06:42:50