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PMID: 17158704 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

Stimulus perception in bacterial signal-transducing histidine kinases.

Microbiology and molecular biology reviews : MMBR ·Vol. 70 ·No. 4 ·2006-12-00 ·Pages 910-38

Mascher T, Helmann JD, Unden G

Abstract

Two-component signal-transducing systems are ubiquitously distributed communication interfaces in bacteria. They consist of a histidine kinase that senses a specific environmental stimulus and a cognate response regulator that mediates the cellular response, mostly through differential expression of target genes. Histidine kinases are typically transmembrane proteins harboring at least two domains: an input (or sensor) domain and a cytoplasmic transmitter (or kinase) domain. They can be identified and classified by virtue of their conserved cytoplasmic kinase domains. In contrast, the sensor domains are highly variable, reflecting the plethora of different signals and modes of sensing. In order to gain insight into the mechanisms of stimulus perception by bacterial histidine kinases, we here survey sensor domain architecture and topology within the bacterial membrane, functional aspects related to this topology, and sequence and phylogenetic conservation. Based on these criteria, three groups of histidine kinases can be differentiated. (i) Periplasmic-sensing histidine kinases detect their stimuli (often small solutes) through an extracellular input domain. (ii) Histidine kinases with sensing mechanisms linked to the transmembrane regions detect stimuli (usually membrane-associated stimuli, such as ionic strength, osmolarity, turgor, or functional state of the cell envelope) via their membrane-spanning segments and sometimes via additional short extracellular loops. (iii) Cytoplasmic-sensing histidine kinases (either membrane anchored or soluble) detect cellular or diffusible signals reporting the metabolic or developmental state of the cell. This review provides an overview of mechanisms of stimulus perception for members of all three groups of bacterial signal-transducing histidine kinases.

MeSH Terms
Bacterial Physiological Phenomena Bacterial Proteins/genetics,physiology Histidine Kinase Protein Kinases/physiology Signal Transduction/physiology
Chemicals
Bacterial Proteins Protein Kinases Histidine Kinase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mascher Thorsten
Department of General Microbiology, Georg-August-University, Grisebachstr. 8, D-37077 Göttingen, Germany. tmasche@gwdg.de
Helmann John D
Unden Gottfried
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Article Info
Journal
Microbiology and molecular biology reviews : MMBR
Abbr.
Microbiol Mol Biol Rev
ISSN
1092-2172
DOI
10.1128/MMBR.00020-06
Email
tmasche@gwdg.de
Published
2006-12-00
Pages
910-38
Language
English
Region
United States
NLM ID
9706653
PMCID
PMC1698512
Subset
IM
Grants
NIGMS NIH HHS · R01 GM047446 · United States
NIGMS NIH HHS · GM047446 · United States
External Links
PubMed source DOI: 10.1128/MMBR.00020-06 PMC Full Text View journal details
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