MMBR Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mascher, T.
Right arrow Articles by Unden, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mascher, T.
Right arrow Articles by Unden, G.
Microbiology and Molecular Biology Reviews, December 2006, p. 910-938, Vol. 70, No. 4
1092-2172/06/$08.00+0     doi:10.1128/MMBR.00020-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

Thorsten Mascher,1* John D. Helmann,2 and Gottfried Unden3*

Department of General Microbiology, Georg-August-University Göttingen, D-37077 Göttingen, Germany,1 Department of Microbiology, Cornell University, Ithaca, New York 14853-8101,2 Institute of Microbiology and Wine Research, Johannes-Gutenberg-University Mainz, D-55099 Mainz, Germany3

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.


* Corresponding author. Mailing address for Thorsten Mascher: Georg-August-University, Dept. of General Microbiology, Grisebachstr. 8, D-37077 Göttingen, Germany. Phone: 49 (0) 551-3919862. Fax: 49 (0) 551-393808. E-mail: tmasche{at}gwdg.de. Mailing address for Gottfried Unden: Johannes-Gutenberg-University, Institute of Microbiology and Wine Research, Becherweg 15, D-55128 Mainz, Germany. Phone: 49 (0) 6131-39-23550. Fax: 49 (0) 6131-39-22695. E-mail: unden{at}uni-mainz.de.


Microbiology and Molecular Biology Reviews, December 2006, p. 910-938, Vol. 70, No. 4
1092-2172/06/$08.00+0     doi:10.1128/MMBR.00020-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. J. Bacteriol.
ALL ASM JOURNALS

Copyright © 2006 by the American Society for Microbiology. All rights reserved.