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Titolo:
The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1
Autore:
Yang, WM; Yao, YL; Seto, E;
Indirizzi:
Univ S Florida, H Lee Moffitt Canc Ctr & Res Inst, Tampa, FL 33612 USA Univ S Florida Tampa FL USA 33612 anc Ctr & Res Inst, Tampa, FL 33612 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 17, volume: 20, anno: 2001,
pagine: 4814 - 4825
SICI:
0261-4189(20010903)20:17<4814:TFP2FA>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAPAMYCIN-BINDING-PROTEIN; CIS-TRANS ISOMERASES; SACCHAROMYCES-CEREVISIAE; CYCLOPHILIN-A; REPRESSION; GENE; IMMUNOPHILINS; MECHANISMS; CLONING; FAMILY;
Keywords:
FK506-binding protein; histone deacetylase; peptidylprolyl cis-trans isomerase; transcription factor YY1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Seto, E Univ S Florida, H Lee Moffitt Canc Ctr & Res Inst, Tampa, FL 33612USA Univ S Florida Tampa FL USA 33612 & Res Inst, Tampa, FL 33612 USA
Citazione:
W.M. Yang et al., "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1", EMBO J, 20(17), 2001, pp. 4814-4825

Abstract

FK506-binding proteins (FKBPs) are cellular receptors for immunosuppressants that belong to a subgroup of proteins, known as immunophilins, with peptidylprolyl cis-trans isomerase (PPIase) activity. Sequence comparison suggested that the HD2-type histone deacetylases and the FKBP-type PPIases may have evolved from a common ancestor enzyme. Here we show that FKBP25 physically associates with the histone deacetylases HDAC1 and HDAC2 and with the HDAC-binding transcriptional regulator YY1. An FKBP25 immunoprecipitated complex contains deacetylase activity, and this activity is associated with the N-terminus of FKBP25, distinct from the FK506/rapamycin-binding domain. Furthermore, FKBP25 can alter the DNA-binding activity of YY1. Together, ourdata firmly establish a relationship between histone deacetylases and the FKBP enzymes and provide a novel and critical function for the FKBPs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 13:17:51