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Science 4 September 1992:
Vol. 257. no. 5075, pp. 1395 - 1398
DOI: 10.1126/science.1382312
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Articles

Science, Vol 257, Issue 5075, 1395-1398
Copyright © 1992 by American Association for the Advancement of Science

articles

Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation

O Amster-Choder and A Wright

Department of Molecular Biology and Microbiology, Tufts University Health Sciences Campus, Boston, MA 02111.

The transcriptional antiterminator protein BglG inhibits transcription termination of the bgl operon in Escherichia coli when it is in the nonphosphorylated state. The BglG protein is now shown to exist in two configurations, an active, dimeric nonphosphorylated form and an inactive, monomeric phosphorylated form. The migration of BglG on native polyacrylamide gels was consistent with it existing as a dimer when nonphosphorylated and as a monomer when phosphorylated. Only the nonphosphorylated dimer was found to bind to the target RNA. When the dimerization domain of the lambda repressor was replaced with BglG, the resulting chimera behaved like an intact lambda repressor in its ability to repress lambda gene expression, which suggests that BglG dimerizes in vivo. Repression by the lambda-BglG hybrid was significantly reduced by BglF, the BglG kinase, an effect that was relieved by conditions that stimulate dephosphorylation of BglG by BglF. These results suggest that the phosphorylation and the dephosphorylation of BglG regulate its activity by controlling its dimeric state.


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