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A Regulatory Protein That Interferes with Activator-Stimulated Transcription in Bacteria

Transcriptional activator proteins in bacteria often operate by interaction with the C-terminal domain of the α-subunit of RNA polymerase (RNAP). Here we report the discovery of an "anti-α" factor Spx in Bacillus subtilis that blocks transcriptional activation by binding to the α-C-termina...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2003-04, Vol.100 (7), p.4233-4238
Main Authors: Nakano, Shunji, Nakano, Michiko M., Zhang, Ying, Leelakriangsak, Montira, Zuber, Peter
Format: Article
Language:English
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Summary:Transcriptional activator proteins in bacteria often operate by interaction with the C-terminal domain of the α-subunit of RNA polymerase (RNAP). Here we report the discovery of an "anti-α" factor Spx in Bacillus subtilis that blocks transcriptional activation by binding to the α-C-terminal domain, thereby interfering with the capacity of RNAP to respond to certain activator proteins. Spx disrupts complex formation between the activator proteins ResD and ComA and promoter-bound RNAP, and it does so by direct interaction with the α-subunit. ResD- and ComA-stimulated transcription requires the proteolytic elimination of Spx by the ATP-dependent protease ClpXP. Spx represents a class of transcriptional regulators that inhibit activator-stimulated transcription by interaction with α.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0637648100