The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein.

Members of the four-and-a-half-LIM domain (FHL) protein family, which are expressed in a tissue- and stage-specific manner, have been reported previously to function as transcriptional coactivators. One of these is the p53-inducible protein DRAL/FHL2 (where DRAL is down-regulated in rhabdomyosarcoma LIM domain protein). In this work, we identified potential binding ...
partners for DRAL/FHL2 using an inducible yeast two-hybrid system. We present evidence of a functional interaction between the promyelocytic leukemia zinc finger protein (PLZF) and DRAL/FHL2. PLZF is a sequence-specific transcriptional repressor whose function relies on recruitment of corepressors that form part of the histone deacetylase complex involved in chromatin remodeling. DRAL/FHL2 interacts specifically with PLZF in vitro and in vivo and augments transcriptional repression mediated by PLZF. This is the first reported incidence of a bona fide FHL protein-mediated corepression and supports the notion of these proteins having a role as coregulators of tissue-specific gene expression.
Mesh Terms:
Antigens, Polyomavirus Transforming, Cloning, Molecular, DNA-Binding Proteins, Glutathione Transferase, Homeodomain Proteins, Humans, Kruppel-Like Transcription Factors, Muscle Proteins, Neoplasm Proteins, Recombinant Proteins, Repressor Proteins, Saccharomyces cerevisiae, Transcription Factors, U937 Cells, Zinc Fingers
J. Biol. Chem.
Date: Oct. 04, 2002
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