A Novel Member of the BTB/POZ Family, PATZ, Associates with the RNF4 RING Finger Protein and Acts as a Transcriptional Repressor

We have identified a novel human gene encoding a 59-kDa POZ-AT hook-zinc finger protein (PATZ) that interacts with RNF4, a mediator of androgen receptor activity, and acts as a transcriptional repressor. PATZ cDNA was isolated through a two-hybrid interaction screening using the RING finger protein...

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Published inThe Journal of biological chemistry Vol. 275; no. 11; pp. 7894 - 7901
Main Authors Fedele, Monica, Benvenuto, Giovanna, Pero, Raffaela, Majello, Barbara, Battista, Sabrina, Lembo, Francesca, Vollono, Erminia, Day, Patricia M., Santoro, Massimo, Lania, Luigi, Bruni, Carmelo Bruno, Fusco, Alfredo, Chiariotti, Lorenzo
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 17.03.2000
American Society for Biochemistry and Molecular Biology
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Summary:We have identified a novel human gene encoding a 59-kDa POZ-AT hook-zinc finger protein (PATZ) that interacts with RNF4, a mediator of androgen receptor activity, and acts as a transcriptional repressor. PATZ cDNA was isolated through a two-hybrid interaction screening using the RING finger protein RNF4 as a bait.In vitro and in vivo interaction between RNF4 and PATZ was demonstrated by protein-protein affinity chromatography and coimmunoprecipitation experiments. Such interaction occurred through a small region of PATZ containing an AT-hook DNA binding domain. Immunofluorescence staining and confocal microscopy showed that PATZ localizes in distinct punctate nuclear regions and colocalizes with RNF4. Functional analysis was performed by cotransfection assays: PATZ acted as a transcriptional repressor, whereas its partner RNF4 behaved as a transcriptional activator. When both proteins were overexpressed a strong repression of the basal transcription was observed, indicating that the association of PATZ with RNF4 switches activation to repression. In addition, RNF4 was also found to associate with HMGI(Y), a chromatin-modeling factor containing AT-hook domains.
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ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.275.11.7894