A Novel RNA Polymerase-binding Protein that interacts with a Sigma-Factor Docking Site

TY - JOUR

T1 - A Novel RNA Polymerase-binding Protein that interacts with a Sigma-Factor Docking Site

AU - Wang Erickson, Anna F

AU - Deighan, Padraig

AU - Chen, Shanshan

AU - Barrasso, Kelsey

AU - Garcia, Cinthia P

AU - Martínez-Lumbreras, Santiago

AU - Alfano, Caterina

AU - Krysztofinska, Ewelina M

AU - Thapaliya, Arjun

AU - Camp, Amy H

AU - Isaacson, Rivka L

AU - Hochschild, Ann

AU - Losick, Richard

N1 - © 2017 John Wiley & Sons Ltd.

PY - 2017/6/19

Y1 - 2017/6/19

N2 - Sporulation in Bacillus subtilis is governed by a cascade of alternative RNA polymerase sigma factors. We previously identified a small protein Fin that is produced under the control of the sporulation sigma factor σ(F) to create a negative feedback loop that inhibits σ(F) -directed gene transcription. Cells deleted for fin are defective for spore formation and exhibit increased levels of σ(F) -directed gene transcription. Based on pull-down experiments, chemical crosslinking, bacterial two-hybrid experiments, and nuclear magnetic resonance chemical shift analysis, we now report that Fin binds to RNA polymerase and specifically to the coiled-coil region of the β' subunit. The coiled-coil is a docking site for sigma factors on RNA polymerase, and evidence is presented that the binding of Fin and σ(F) to RNA polymerase is mutually exclusive. We propose that Fin functions by a mechanism distinct from that of classic sigma factor antagonists (anti-σ factors), which bind directly to a target sigma factor to prevent its association with RNA polymerase, and instead functions to inhibit σ(F) by competing for binding to the β' coiled-coil. This article is protected by copyright. All rights reserved.

AB - Sporulation in Bacillus subtilis is governed by a cascade of alternative RNA polymerase sigma factors. We previously identified a small protein Fin that is produced under the control of the sporulation sigma factor σ(F) to create a negative feedback loop that inhibits σ(F) -directed gene transcription. Cells deleted for fin are defective for spore formation and exhibit increased levels of σ(F) -directed gene transcription. Based on pull-down experiments, chemical crosslinking, bacterial two-hybrid experiments, and nuclear magnetic resonance chemical shift analysis, we now report that Fin binds to RNA polymerase and specifically to the coiled-coil region of the β' subunit. The coiled-coil is a docking site for sigma factors on RNA polymerase, and evidence is presented that the binding of Fin and σ(F) to RNA polymerase is mutually exclusive. We propose that Fin functions by a mechanism distinct from that of classic sigma factor antagonists (anti-σ factors), which bind directly to a target sigma factor to prevent its association with RNA polymerase, and instead functions to inhibit σ(F) by competing for binding to the β' coiled-coil. This article is protected by copyright. All rights reserved.

KW - Journal Article

U2 - 10.1111/mmi.13724

DO - 10.1111/mmi.13724

M3 - Article

C2 - 28598017

SN - 0950-382X

JO - Molecular Microbiology

JF - Molecular Microbiology

ER -