5MSL

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

5MSL の概要

• エントリーDOI: 10.2210/pdb5msl/pdb
• NMR情報: BMRB: 34082
• 分子名称: Anti-sigma-F factor Fin, ZINC ION (2 entities in total)
• 機能のキーワード: zinc finger, bacillus subtilis, sigma factor, sporulation, transcription
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8751.98

構造登録者

Martinez-Lumbreras, S.,Alfano, C.,Isaacson, R.L. (登録日: 2017-01-05, 公開日: 2017-06-21, 最終更新日: 2024-06-19)

主引用文献

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

実験手法

SOLUTION NMR