The sensor region of the ubiquitous cytosolic sensor kinase, PdtaS, contains PAS and GAF domain sensing modules

Julia Preu, Santosh Panjikar, Preben Morth, Rohan Jaiswal, Prashantha Karunakar, Paul A. Tucker

Research output: Contribution to journalArticleResearchpeer-review

11 Citations (Scopus)

Abstract

Two-component systems, a sensor histidine kinase (HK) and a response regulator (RR), are ubiquitous signaling systems that allow prokaryotes to respond to external challenges. HKs normally have sensing modules and highly conserved cytosolic histidine kinase and ATPase domains. The interaction between the activated phosphohistidine and the cognate RR allows an external signal to be passed from the exterior of gram-positive bacteria (GPB) to the cytoplasm. Orthologs of the PdtaS/PdtaR regulatory system, found in most GPB phyla, are unusual in two respects. The HK is not membrane anchored, and the RR acts at the level of transcriptional antitermination. The structure of the complete sensor region of the cytosolic HK, PdtaS, from Mycobacterium tuberculosis consists of closely linked GAF and PAS domains. The structure and sequence analysis suggest that the PdtaS/PdtaR regulatory system is structurally equivalent to the EutW/EutV system regulating ethanolamine catabolism in some phyla but that the effector for the PAS domain is not ethanolamine in the Actinobacteria.

Original languageEnglish
Pages (from-to)498-505
Number of pages8
JournalJournal of Structural Biology
Volume177
Issue number2
DOIs
Publication statusPublished - Feb 2012
Externally publishedYes

Keywords

  • Actinobacteria
  • Crystal structure
  • Ethanolamine catabolism
  • GAF domain
  • Mycobacterium tuberculosis
  • PAS domain
  • PdtaR/PdtaS two-component system
  • Sensor histidine kinase

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