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(Received for publication, July 8, 1997)
From the 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.
Volume 272, Number 39,
Issue of September 26, 1997
pp. 24105-24108
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
,
,
¶
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
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