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Titolo:
DNA-BINDING AND TRANSCRIPTIONAL ACTIVATION BY THE SKI ONCOPROTEIN MEDIATED BY INTERACTION WITH NFI
Autore:
TARAPORE P; RICHMOND C; ZHENG GX; COHEN SB; KELDER B; KOPCHICK J; KRUSE U; SIPPEL AE; COLMENARES C; STAVNEZER E;
Indirizzi:
CASE WESTERN RESERVE UNIV,DEPT BIOCHEM CLEVELAND OH 44106 CASE WESTERN RESERVE UNIV,DEPT BIOCHEM CLEVELAND OH 44106 UNIV CINCINNATI,COLL MED,DEPT MOL GENET BIOCHEM & MICROBIOL CINCINNATI OH 45267 OHIO UNIV,EDISON BIOTECHNOL INST ATHENS OH 45701 UNIV FREIBURG,INST BIOL 3 D-79104 FREIBURG GERMANY CLEVELAND CLIN FDN,RES INST,DEPT CANC BIOL CLEVELAND OH 44195
Titolo Testata:
Nucleic acids research
fascicolo: 19, volume: 25, anno: 1997,
pagine: 3895 - 3903
SICI:
0305-1048(1997)25:19<3895:DATABT>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR FACTOR-I; C-SKI; HUMAN ALDOLASE; RETROVIRUS VECTORS; TRANSGENIC MICE; M-PROMOTER; ONCOGENE; PROTEINS; CHICKEN; TRANSFORMATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
P. Tarapore et al., "DNA-BINDING AND TRANSCRIPTIONAL ACTIVATION BY THE SKI ONCOPROTEIN MEDIATED BY INTERACTION WITH NFI", Nucleic acids research, 25(19), 1997, pp. 3895-3903

Abstract

The Ski oncoprotein has been found to bind nonspecifically to DNA in association with unindentified nuclear factors. In addition, Ski has been shown to activate transcription of muscle-specific and viral promoters/enhancers. The present study was undertaken to identify Ski's DNAbinding and transcriptional activation partners by identifying specific DNA binding sites. We used nuclear extracts from a v-Ski-transducedmouse L-cell line and selected Ski-bound sequences from a pool of degenerate oligonucleotides with anti-Ski monoclonal antibodies. Two sequences were identified by this technique. The first (TGGC/ANNNNNT/GCCAA) is the previously identified binding site of the nuclear factor I (NFI) family of transcription factors. The second (TCCCNNGGGA) is the binding site of Olf-1/EBF. By electrophoretic mobility shift assays we find that Ski is a component of one or more NFI complexes but we fail to detect Ski in Olf-1/EBF complexes. We show that Ski binds NFI proteins and activates transcription of NFI reporters, but only in the presence of NFI. We also find that homodimerization of Ski is essential forco-activation with NFI. However, the C-terminal dimerization domain of c-Ski, which is missing in v-Ski, can be substituted by the leucine zipper domain of GCN4.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 07:58:54