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Titolo:
MEMBERS OF THE MEIS1 AND PBX HOMEODOMAIN PROTEIN FAMILIES COOPERATIVELY BIND A CAMP-RESPONSIVE SEQUENCE (CRS1) FROM BOVINE CYP17
Autore:
BISCHOF LJ; KAGAWA N; MOSKOW JJ; TAKAHASHI Y; IWAMATSU A; BUCHBERG AM; WATERMAN MR;
Indirizzi:
VANDERBILT UNIV,SCH MED,DEPT BIOCHEM,221 KIRKLAND HALL NASHVILLE TN 37232 THOMAS JEFFERSON UNIV,JEFFERSON MED COLL,KIMMEL CANC CTR PHILADELPHIAPA 19107 KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 221 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 14, volume: 273, anno: 1998,
pagine: 7941 - 7948
SICI:
0021-9258(1998)273:14<7941:MOTMAP>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN PROTOONCOGENE PBX1; DNA-BINDING; HOX PROTEINS; TRANSCRIPTIONAL REGULATION; HOMEOBOX GENES; PRE-B; EXTRADENTICLE; MOTIF; SPECIFICITY; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
L.J. Bischof et al., "MEMBERS OF THE MEIS1 AND PBX HOMEODOMAIN PROTEIN FAMILIES COOPERATIVELY BIND A CAMP-RESPONSIVE SEQUENCE (CRS1) FROM BOVINE CYP17", The Journal of biological chemistry, 273(14), 1998, pp. 7941-7948

Abstract

The mammalian Pbx homeodomain proteins provide specificity and increased DNA binding affinity to other homeodomain proteins, A cAMP-responsive sequence (CRS1) from bovine CYP17 has previously been shown to be a binding site for Pbx1, A member of a second mammalian homeodomain family, Meis1, is now also demon strated to be a CRS1-binding protein upon purification using CRS1 affinity chromatography, CRS1 binding complexes from Y1 adrenal cell nuclear extract contain both Pbx1 and Meis1,This is the first transcriptional regulatory element reported as a binding site for members of the Meis1 homeodomain family. Pbx1 and Meis1bind cooperatively to CRS1, whereas neither protein can bind this element alone. Mutagenesis of the CRS1 element indicates a binding site for Meis1 adjacent to the Pbx site, All previously identified Pbx binding partners have Pbx interacting motifs that contain a tryptophan residue amino-terminal to the homeodomain that is required for cooperativebinding to DNA with Pbx. Members of the Meis1 family contain one tryptophan residue amino-terminal to the homeodomain, but site-directed mutagenesis indicates that this residue is not required for cooperative CRS1 binding with Pbx, Thus, the Pbx-Meis1 interaction is unique amongPbx complexes. Meis1 also cooperatively binds CRS1 with the Pbx homologs extradenticle from Drosophila melanogaster and ceh-20 from Caenorhabditis elegans, indicating that this interaction is evolutionarily conserved, Thus, CYP17 CRS1 is a transcriptional regulatory element containing both Pbx and Meis1 binding sites, which permit these two homeodomain proteins to bind and potentially regulate cAMP-dependent transcription through this sequence.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:31:06