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Titolo:
PROTEINS BINDING TO 5' UNTRANSLATED REGION SITES - A GENERAL MECHANISM FOR TRANSLATIONAL REGULATION OF MESSENGER-RNAS IN HUMAN-CELLS AND YEAST-CELLS
Autore:
STRIPECKE R; OLIVEIRA CC; MCCARTHY JEG; HENTZE MW;
Indirizzi:
EUROPEAN MOLEC BIOL LAB,GENE EXPRESS PROGRAMME,MEYERHOFSTR 1 D-69117 HEIDELBERG GERMANY EUROPEAN MOLEC BIOL LAB,GENE EXPRESS PROGRAMME D-69117 HEIDELBERG GERMANY GESELL BIOTECHNOL FORSCH MBH,DEPT GENE EXPRESS D-38124 BRAUNSCHWEIG GERMANY
Titolo Testata:
Molecular and cellular biology
fascicolo: 9, volume: 14, anno: 1994,
pagine: 5898 - 5909
SICI:
0270-7306(1994)14:9<5898:PBT5UR>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
IRON-RESPONSIVE ELEMENTS; FERRITIN MESSENGER-RNA; SECONDARY STRUCTURE; ESCHERICHIA-COLI; U1A PROTEIN; SACCHAROMYCES-CEREVISIAE; PREMESSENGER RNA; A-PROTEIN; REPRESSION; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
R. Stripecke et al., "PROTEINS BINDING TO 5' UNTRANSLATED REGION SITES - A GENERAL MECHANISM FOR TRANSLATIONAL REGULATION OF MESSENGER-RNAS IN HUMAN-CELLS AND YEAST-CELLS", Molecular and cellular biology, 14(9), 1994, pp. 5898-5909

Abstract

We demonstrate that a bacteriophage protein and a spliceosomal protein can be converted into eukaryotic translational repressor proteins. mRNAs with binding sites for the bacteriophage MS2 coat protein or the spliceosomal human U1A protein were expressed in human HeLa cells and yeast. The presence of the appropriate binding protein resulted in specific, dose-dependent translational repression when the binding sites were located in the 5' untranslated region (UTR) of the reporter mRNAs. Neither mRNA esport from the nucleus to the cytoplasm nor mRNA stability was demonstrably affected by the binding proteins. The dots thus reveal a general mechanism for translational regulation: formation of mRNA-protein complexes in the 5' UTR controls translation initiation by steric blockage of a sensitive step in the initiation pathway. Moreover, the findings establish the basis for novel strategies to study RNA-protein interactions in vivo and to clone RNA-binding proteins.

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Documento generato il 02/10/20 alle ore 00:37:56