The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor.
The TRPS1 gene encodes a repressor of GATA-mediated transcription. Mutations in this gene cause the tricho-rhino-phalangeal syndromes, but the affected pathways are unknown. In a yeast two-hybrid screen with the C-terminal part of the murine Trps1 protein as bait, we obtained three yeast clones encoding two overlapping fragments of the 194 amino acids RING finger protein 4 ( Rnf4). The overlap narrows down the Trps1- binding region within Rnf4 to amino acids 6-65. This region in Rnf4 is also known to interact with several proteins including steroid receptors. By using truncated Trps1 constructs, the Rnf4- binding region in Trps1 could be assigned to amino acids 985-1184 of 1281. This 200 amino acid region of Trps1 does not contain any predicted protein-protein interacting motif. Complex formation between the human proteins TRPS1 and RNF4 was verified by co-immunoprecipitation from transfected and native mammalian cells. Confocal laser-scanning microscopy revealed that the endogenous proteins are located in distinct structures of the nucleus. Using a luciferase reporter assay, we could demonstrate that the repressional function of TRPS1 is inhibited by RNF4. This finding suggests that RNF4 is a negative regulator of TRPS1 activity.[1]References
- The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor. Kaiser, F.J., Möröy, T., Chang, G.T., Horsthemke, B., Lüdecke, H.J. J. Biol. Chem. (2003) [Pubmed]
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