5MSL

Solution structure of the B. subtilis anti-sigma-F factor, FIN

Summary for 5MSL

• Entry DOI: 10.2210/pdb5msl/pdb
• NMR Information: BMRB: 34082
• Descriptor: Anti-sigma-F factor Fin, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, bacillus subtilis, sigma factor, sporulation, transcription
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 8751.98

Authors

Martinez-Lumbreras, S.,Alfano, C.,Isaacson, R.L. (deposition date: 2017-01-05, release date: 2017-06-21, Last modification date: 2024-06-19)

Primary citation

Wang Erickson, A.F.,Deighan, P.,Chen, S.,Barrasso, K.,Garcia, C.P.,Martinez-Lumbreras, S.,Alfano, C.,Krysztofinska, E.M.,Thapaliya, A.,Camp, A.H.,Isaacson, R.L.,Hochschild, A.,Losick, R.
A novel RNA polymerase-binding protein that interacts with a sigma-factor docking site.
Mol. Microbiol., 105:652-662, 2017

PubMed Abstract: 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 to create a negative feedback loop that inhibits σ -directed gene transcription. Cells deleted for fin are defective for spore formation and exhibit increased levels of σ -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 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 by competing for binding to the β' coiled-coil.

PubMed: 28598017
DOI: 10.1111/mmi.13724

Experimental method

SOLUTION NMR