7T5U

Structure of E. coli MS115-1 CapH N-terminal domain

7T5U の概要

• エントリーDOI: 10.2210/pdb7t5u/pdb
• 分子名称: Helix-turn-helix domain-containing protein, SULFATE ION (3 entities in total)
• 機能のキーワード: helix turn helix, hth, ddro, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7870.80

構造登録者

Lau, R.K.,Corbett, K.D. (登録日: 2021-12-13, 公開日: 2022-09-14, 最終更新日: 2024-04-03)

主引用文献

Lau, R.K.,Enustun, E.,Gu, Y.,Nguyen, J.V.,Corbett, K.D.
A conserved signaling pathway activates bacterial CBASS immune signaling in response to DNA damage.
Embo J., 41:e111540-e111540, 2022

PubMed Abstract: To protect themselves from the constant threat of bacteriophage (phage) infection, bacteria have evolved diverse immune systems including restriction-modification, CRISPR-Cas, and many others. Here, we describe the discovery of a two-protein transcriptional regulator module associated with hundreds of CBASS immune systems and demonstrate that this module drives the expression of its associated CBASS system in response to DNA damage. We show that the helix-turn-helix transcriptional repressor CapH binds the promoter region of its associated CBASS system to repress transcription until it is cleaved by the metallopeptidase CapP. CapP is activated in vitro by single-stranded DNA, and in cells by DNA-damaging drugs. Together, CapH and CapP drive increased expression of their associated CBASS system in response to DNA damage. We identify CapH- and CapP-related proteins associated with diverse known and putative bacterial immune systems including DISARM and Pycsar antiphage operons. Overall, our data highlight a mechanism by which bacterial immune systems can sense and respond to a universal signal of cell stress, potentially enabling multiple immune systems to mount a coordinated defensive response against an invading pathogen.

PubMed: 36156805
DOI: 10.15252/embj.2022111540

実験手法

X-RAY DIFFRACTION (1.02 Å)