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Volume 272, Number 39, Issue of September 26, 1997 pp. 24105-24108
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Interaction of WW Domains with Hematopoietic Transcription Factor p45/NF-E2 and RNA Polymerase II

(Received for publication, July 8, 1997)

Narender R. Gavva Dagger , Rama Gavva Dagger , Kira Ermekova § , Marius Sudol § and C.-K. James Shen Dagger

From the Dagger  Section of Molecular and Cellular Biology, University of California, Davis, California 95616, the § Department of Biochemistry, Mount Sinai School of Medicine, New York, New York 10029, and the  Institute of Molecular Biology, Academia Sinica, Taipei 11529, Republic of China

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.


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