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Titolo:
SCHIZOSACCHAROMYCES-POMBE HAS A NOVEL EUKARYOTIC INITIATION-FACTOR 4FCOMPLEX CONTAINING A CAP-BINDING PROTEIN WITH THE HUMAN EIF4E C-TERMINAL MOTIF KSGST
Autore:
PTUSHKINA M; FIERROMONTI I; VANDENHEUVEL J; VASILESCU S; BIRKENHAGER R; MITA K; MCCARTHY JEG;
Indirizzi:
UMIST,DEPT BIOCHEM,POB 88 MANCHESTER M60 1QD LANCS ENGLAND NATL BIOTECHNOL RES CTR,DEPT GENE EXPRESS D-38124 BRAUNSCHWEIG GERMANY NATL INST RADIOL SCI,GENOME RES GRP,INAGE KU CHIBA 260 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 51, volume: 271, anno: 1996,
pagine: 32818 - 32824
SICI:
0021-9258(1996)271:51<32818:SHANEI>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESSENGER-RNA; SACCHAROMYCES-CEREVISIAE; FACTOR EIF-4E; TRANSLATIONAL INITIATION; SECONDARY STRUCTURE; YEAST; PHOSPHORYLATION; GENES; RECOGNITION; SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
M. Ptushkina et al., "SCHIZOSACCHAROMYCES-POMBE HAS A NOVEL EUKARYOTIC INITIATION-FACTOR 4FCOMPLEX CONTAINING A CAP-BINDING PROTEIN WITH THE HUMAN EIF4E C-TERMINAL MOTIF KSGST", The Journal of biological chemistry, 271(51), 1996, pp. 32818-32824

Abstract

Genetic and biochemical analyses mere performed on the cytoplasmic cap-binding complex (eukaryotic initiation factor (eIF) 4F) of Schizosaccharomyces pombe, Genomic and cDNA sequencing of the S. pombe gene (tif1) encoding the cap-binding component eIF4E revealed the presence of two introns in a reading frame of 219 codons. The encoded sequence of 218 amino acids shows a greater degree of identity to the mammalian eIF4E sequence than does its counterpart from Saccharomyces cerevisiae, In particular, unlike its S. cerevisiae counterpart, S.pombe eIF4E hasa C-terminal Ser(209) within the motif KSGST that is a site of phosphorylation in hamster and rabbit eIF4E. Of relevance to its potential regulatory role, eIF4E was found to be encoded by an mRNA with a six-nucleotide leader and to be of low abundance in vivo. Cross-linking experiments identified S. pombe eIF4E as the major cap binding protein while a further protein, p36, also showed cap-dependent binding. eIF4A was not associated with the cap-binding complex. While S. pombe eIF4E was shown capable of binding S. cerevisiae p20, an equivalent protein was absent from the eIF4F complex isolated from S. pombe cells. S. pombe4F therefore shows a remarkable combination of structural and functional properties, some of which it shares with its higher and its lower eukaryotic counterparts.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 07:13:04