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Titolo:
Oncogenic transformation by the FOX protein Qin requires DNA binding
Autore:
Ma, Y; Geerdes, DW; Vogt, PK;
Indirizzi:
Scripps Res Inst, Dept Mol & Expt Med, Div Oncovirol, La Jolla, CA 92037 USA Scripps Res Inst La Jolla CA USA 92037 Oncovirol, La Jolla, CA 92037 USA
Titolo Testata:
ONCOGENE
fascicolo: 42, volume: 19, anno: 2000,
pagine: 4815 - 4821
SICI:
0950-9232(20001005)19:42<4815:OTBTFP>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTORS; CEREBRAL HEMISPHERES; FORK HEAD; EXPRESSION; FAMILY; BF-1; DOMAINS; RETINA; BRAIN;
Keywords:
Qin; BF-1 oncogenic transformation; winged helix domain/forkhead box; DNA binding; transcriptional repression;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Vogt, PK Scripps Res Inst, Dept Mol & Expt Med, Div Oncovirol, 10550 N Torrey PinesRd, La Jolla, CA 92037 USA Scripps Res Inst 10550 N Torrey Pines Rd La Jolla CA USA 92037 SA
Citazione:
Y. Ma et al., "Oncogenic transformation by the FOX protein Qin requires DNA binding", ONCOGENE, 19(42), 2000, pp. 4815-4821

Abstract

Some functions of the Qin oncoprotein are not dependent on DNA binding, Inorder to test the requirement for DNA binding in Qin-induced oncogenic transformation, site directed mutations were introduced in the winged helix (WH) DNA binding domain of the Qin protein, In cellular Qin (c-Qin), the glycine at position 233 was either deleted or substituted with the amino acids aspartic acid, alanine, glutamic acid, asparagine, proline or lysine, The same position carries aspartic acid in the viral Qin protein (v-Qin), The adjacent residues, threonine 232 and lysine 234, were separately mutated to proline, Several additional amino acid substitutions believed to be involvedin DNA contacts were introduced at the following c-Qin positions: asparagine 189, histidine 193, serine 196 or arginine 236, Most of the substitutions reduced DNA binding of Qin, one mutation, H193A, completely abolished DNAbinding, and another mutation, T232P, increased DNA binding affinity, Mutant H193A failed to transform chicken embryo fibroblasts (CEF), all other mutants, even those showing minimal DNA binding, retained oncogenicity for CEF, The efficiencies of focus formation induced by these mutant proteins in cell culture were not significantly different from that of wild type, However, the rate of focus development and the size of foci induced by the Qin mutants were greater with strong DNA binders than with weak DNA binders, Transdominant negative constructs consisting of the winged helix domain of c-Qin or v-Qin interfered with focus formation induced by full length Qin proteins, These results suggest that DNA binding is a prerequisite for transformation by Qin, and strong DNA binding is related to accelerated transformation in CEF.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 10:13:54