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Mol. Cell. Biol., Dec 1996, 6900-6908, Vol 16, No. 12
Copyright © 1996, American Society for Microbiology

Phosphorylation of E47 as a potential determinant of B-cell-specific activity

SR Sloan, CP Shen, R McCarrick-Walmsley and T Kadesch
Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.

The E2A gene encodes two basic helix-loop-helix proteins designated E12 and E47. Although these proteins are widely expressed, they are required only for the B-lymphocyte lineage where DNA binding is mediated distinctively by E47 homodimers. By studying the properties of deltaE47, an N-terminal truncation of E47, we provide evidence that phosphorylation may contribute to B-cell-specific DNA binding by E47. Two serines N terminal to the deltaE47 basic helix-loop-helix domain were found to be phosphorylated in a variety of cell types but were hypophosphorylated in B cells. Phosphorylating these serines in vitro inhibited DNA binding by deltaE47 homodimers but not by deltaE47- containing heterodimers, such as deltaE47:MyoD. These results argue that hypophosphorylation may be a prerequisite for activity of E47 homodimers in B cells, suggesting the use of an inductive (nonstochastic) step in early B-cell development.


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