Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1.

@article{Bhattacharya1999FunctionalRO,
  title={Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1.},
  author={Shoumo Bhattacharya and Christian Michels and Mike W. K. Leung and Zoltan Arany and Andrew L Kung and David Livingston},
  journal={Genes & development},
  year={1999},
  volume={13 1},
  pages={
          64-75
        }
}
Recruitment of p300/CBP by the hypoxia-inducible factor, HIF-1, is essential for the transcriptional response to hypoxia and requires an interaction between the p300/CBP CH1 region and HIF-1alpha. A new p300-CH1 interacting protein, p35srj, has been identified and cloned. p35srj is an alternatively spliced isoform of MRG1, a human protein of unknown function. Virtually all endogenous p35srj is bound to p300/CBP in vivo, and it inhibits HIF-1 transactivation by blocking the HIF-1alpha/p300 CH1… CONTINUE READING
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