Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II.
NF-E2 is an erythroid-specific transcription factor required for expression of several erythroid-specific genes. By Far-Western blotting and yeast two-hybrid assay, we demonstrate that p45, the large subunit of NF-E2, is capable of binding to a specific set of WW domain-containing proteins, including the ubiquitin ligase hRPF1. This binding is mediated ... through the interaction between the WW domains and a PY motif located within the amino-terminal region of p45. Interestingly, the carboxyl-terminal domain of mammalian RNA polymerase II binds a similar set of WW domains to which p45 interacts with. We discuss the data in terms of possible new pathways through which the processes of transcriptional regulation by NF-E2 could be regulated in erythroid and megakaryote cells.
Mesh Terms:
Amino Acid Sequence, Bone Marrow, DNA-Binding Proteins, Erythroid-Specific DNA-Binding Factors, Molecular Sequence Data, NF-E2 Transcription Factor, NF-E2 Transcription Factor, p45 Subunit, Protein Binding, RNA Polymerase II, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Transcription Factors
Amino Acid Sequence, Bone Marrow, DNA-Binding Proteins, Erythroid-Specific DNA-Binding Factors, Molecular Sequence Data, NF-E2 Transcription Factor, NF-E2 Transcription Factor, p45 Subunit, Protein Binding, RNA Polymerase II, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Transcription Factors
J. Biol. Chem.
Date: Sep. 26, 1997
PubMed ID: 9305852
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