Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation

Orna Amster-Choder*, Andrew Wright

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

116 Scopus citations

Abstract

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 λ repressor was replaced with BglG, the resulting chimera behaved like an intact λ repressor in its ability to repress λ gene expression, which suggests that BglG dimerizes in vivo. Repression by the λ-BglG hybrid was significantly reduced by BgF 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.

Original languageAmerican English
Pages (from-to)1395-1398
Number of pages4
JournalScience
Volume257
Issue number5075
StatePublished - 4 Sep 1992
Externally publishedYes

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