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J Biol Chem, Vol. 274, Issue 2, 1040-1049, January 8, 1999
From the Cell Biology Program, Memorial Sloan-Kettering Cancer
Center, New York, New York 10021
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.
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