Two isoforms of protein disulfide isomerase alter the dimerization status of E2A proteins by a redox mechanism Journal Article
| Authors: | Markus, M.; Benezra, R. |
| Article Title: | Two isoforms of protein disulfide isomerase alter the dimerization status of E2A proteins by a redox mechanism |
| Abstract: | We have shown previously that E2A helix-loop-helix proteins spontaneously form an intermolecular disulfide cross-link that is required for stable homodimer binding to DNA (Benezra, R. (1994) Cell 79, 1057-1067). These homodimers are important for the development of B lymphocytes but are not present in other cell lineages. We have purified two proteins that are capable of regulating the formation of this disulfide bond and found them to be members of the protein disulfide isomerase (PDI) family. By regulating the formation of the disulfide cross-link, these proteins are capable of regulating the dimerization state of E proteins. PDI-mediated reduction appears to dissociate E protein homodimers and favors heterodimer formation with other basic helix-loop-helix proteins in both a purified protein system and in cellular extracts. These studies suggest that PDI may play an important role in the regulation of E2A transcription factor dimerization and the development of the B lymphocyte lineage. |
| Keywords: | controlled study; human cell; hela cells; b lymphocyte; cell lineage; b-lymphocytes; enzyme regulation; amino acid sequence; molecular sequence data; recombinant proteins; base sequence; dimerization; dna primers; protein structure; oxidation reduction reaction; oxidation-reduction; isoenzymes; helix loop helix protein; protein disulfide isomerase; disulfide bond; protein disulfide-isomerase; oxidation reduction state; humans; human; priority journal; article; adenovirus e2 proteins |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 274 |
| Issue: | 2 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1999-01-08 |
| Start Page: | 1040 |
| End Page: | 1049 |
| Language: | English |
| DOI: | 10.1074/jbc.274.2.1040 |
| PUBMED: | 9873049 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
