Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II

Narender R. Gavva, Rama Gavva, Kira Ermekova, Marius Sudol, C. K.James Shen

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)24105-24108
Number of pages4
JournalJournal of Biological Chemistry
Volume272
Issue number39
DOIs
Publication statusPublished - Sep 26 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II'. Together they form a unique fingerprint.

  • Cite this