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A coiled-coil from the RNA polymerase beta' subunit allosterically induces selective nontemplate strand binding by sigma(sup)70

Article Abstract:

Results indicate that the beta' coiled-coil and sigma(sup)70 region interact and promote an allosteric transition that enables sigma(sup)70 to selectively recognize the nontemplate strand. Data reveal that a 48 amino acid coiled-coil of the beta' subunit induces sigma(sup)70 to perform the task as efficiently as core RNA polymerase.

Author: Burgess, Richard R., Arthur, Terrance M., Young, Brian A., Anthony, Larry C., Gruber, Tanja M., Heyduk, Ewa, Lu, Chi Zen, Sharp, Meghan M., Heyduk, Tomasz, Gross, Carol A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
Enzymes, Genetic regulation, RNA polymerases, Enzyme structure-activity relationships, Allosteric enzymes

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Luminescence resonance energy transfer-based high-throughput screening assay for inhibitors of essential protein-protein interactions in bacterial RNA polymerase

Article Abstract:

This article describes a homogeneous assay for sigma factor binding to RNA polymerase based on luminescence resonance energy transfer. Data indicate that the assay can be performed in a multiwell plate and read by amultiplate reader enabling it to be a robust high-throughput screening assay for protein-proein interaction.

Author: Burgess, Richard R., Heyduk, Tomasz, Bergendahl, Veit
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
Methods, Measurement, Proteins, Luminescence, Resonance, Resonance (Physics), Assaying

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OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain

Article Abstract:

Results show that outer-membrane porins-like C-terminal sequences bind to DegS protease PDZ domain and activate DegS cleavage of transmembrane protein RseA to induce sigma(sup)E -dependent transcription. Data indicate that DegS senses envelope stress by binding to unassembled outer membrane porins.

Author: Gross, Carol A., Sauer, Robert T., Walsh, Nathan P., Alba, Benjamin M., Bose, Baundauna
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
Membrane proteins, Cellular signal transduction, Enzyme activation, Porins

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Subjects list: United States, Analysis, Physiological aspects, Genetic transcription, Transcription (Genetics)
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