| First Author | Gavva NR | Year | 1997 |
| Journal | J Biol Chem | Volume | 272 |
| Issue | 39 | Pages | 24105-8 |
| PubMed ID | 9305852 | Mgi Jnum | J:140926 |
| Mgi Id | MGI:3814925 | Doi | 10.1074/jbc.272.39.24105 |
| Citation | Gavva NR, et al. (1997) Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II. J Biol Chem 272(39):24105-8 |
| abstractText | 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. |
