Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Heterodimers of the SnoN and Ski oncoproteins form preferentially over homodimers and are more potent transforming agents
Autore:
Cohen, SB; Zheng, GX; Heyman, HC; Stavnezer, E;
Indirizzi:
Case Western Reserve Univ, Dept Biochem, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA UnivSAincinnati, Dept Mol Genet Biochem & Microbiol, Cincinnati, OH 45267 U Univ Cincinnati Cincinnati OH USA 45267 Microbiol, Cincinnati, OH 45267 U
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 4, volume: 27, anno: 1999,
pagine: 1006 - 1014
SICI:
0305-1048(19990215)27:4<1006:HOTSAS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-MYC PROTEIN; DNA-BINDING; MUSCLE DIFFERENTIATION; SKELETAL-MUSCLE; CDNA CLONES; MAX; SEQUENCE; GENE; EXPRESSION; ONCOGENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Stavnezer, E Case106stern Reserve Univ, Dept Biochem, 10900 Euclid Ave, Cleveland, OH 44 Case Western Reserve Univ 10900 Euclid Ave Cleveland OH USA 44106
Citazione:
S.B. Cohen et al., "Heterodimers of the SnoN and Ski oncoproteins form preferentially over homodimers and are more potent transforming agents", NUCL ACID R, 27(4), 1999, pp. 1006-1014

Abstract

sno is a member of the ski oncogene family and shaves ski's ability to transform avian fibroblasts and induce muscle differentiation. Ski and SnoN are transcription factors that form both homodimers and heterodimers. They recognize a specific DNA binding site (GTCTAGAC) through which they repress transcription. Efficient homodimerization of Ski, mediated by a bipartite C-terminal domain consisting of five tandem repeats (TR) and a leucine zipper(LZ), correlates with efficient DNA binding and cellular transformation. The present study assesses the role of SnoN homodimerization and SnoN:Ski heterodimerization in the activities of these proteins. Unlike Ski, efficienthomodimerization by SnoN is shown to require an upstream region of the protein in addition to the TR/LZ domain. Deletion of the TR/LZ from SnoN decreases its activity in transcriptional repression and cellular transformation. When coexpressed in vitro, c-Ski and SnoN preferentially form heterodimers. In vivo, they form heterodimers that bind the GTCTAGAC element. TetheredSki:Sno heterodimers that lack TR/LZ domains are more active than either their monomeric counterparts, tethered Ski:Ski homodimers or full-length SnoN and c-Ski, This work demonstrates, for the first time, the differences between dimer formation by Ski and SnoN and underscores the importance of dimerization in their activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 10:38:30