Literature DB >> 20223701

Sensor domains of two-component regulatory systems.

Jonah Cheung1, Wayne A Hendrickson.   

Abstract

Two-component systems regulate crucial cellular processes in microorganisms, and each comprises a homodimeric histidine kinase receptor and a cytoplasmic response regulator. Histidine kinases, often membrane associated, detect environmental input at sensor domains and propagate resulting signals to catalytic cytoplasmic transmitter domains. Recent studies on the great diversity of sensor domains reveal patterns of domain organization and biochemical properties that provide insight into mechanisms of signaling. Despite the enormous sequence variability found within sensor input domains, they fall into a relatively small number of discrete structural classes. Subtle rearrangements along a structurally labile dimer interface, in the form of possible sliding or rotational motions, are propagated from the sensor domain to the transmitter domain to modulate activity of the receptor. Copyright 2010 Elsevier Ltd. All rights reserved.

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Year:  2010        PMID: 20223701      PMCID: PMC3078554          DOI: 10.1016/j.mib.2010.01.016

Source DB:  PubMed          Journal:  Curr Opin Microbiol        ISSN: 1369-5274            Impact factor:   7.934


  57 in total

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Authors:  R Dutta; L Qin; M Inouye
Journal:  Mol Microbiol       Date:  1999-11       Impact factor: 3.501

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3.  Structural plasticity and catalysis regulation of a thermosensor histidine kinase.

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4.  High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.

Authors:  J I Yeh; H P Biemann; G G Privé; J Pandit; D E Koshland; S H Kim
Journal:  J Mol Biol       Date:  1996-09-20       Impact factor: 5.469

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Authors:  W Gong; B Hao; M K Chan
Journal:  Biochemistry       Date:  2000-04-11       Impact factor: 3.162

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7.  Time-resolved crystallographic studies of the heme domain of the oxygen sensor FixL: structural dynamics of ligand rebinding and their relation to signal transduction.

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Authors:  Y S Ho; L M Burden; J H Hurley
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Review 9.  Structure and signaling mechanism of Per-ARNT-Sim domains.

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Journal:  Structure       Date:  2009-10-14       Impact factor: 5.006

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  90 in total

Review 1.  Spatial organization in bacterial chemotaxis.

Authors:  Victor Sourjik; Judith P Armitage
Journal:  EMBO J       Date:  2010-08-18       Impact factor: 11.598

Review 2.  Microbial Surface Colonization and Biofilm Development in Marine Environments.

Authors:  Hongyue Dang; Charles R Lovell
Journal:  Microbiol Mol Biol Rev       Date:  2015-12-23       Impact factor: 11.056

3.  MifS, a DctB family histidine kinase, is a specific regulator of α-ketoglutarate response in Pseudomonas aeruginosa PAO1.

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Journal:  Microbiology (Reading)       Date:  2020-09       Impact factor: 2.777

4.  Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor.

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Journal:  Proc Natl Acad Sci U S A       Date:  2017-03-06       Impact factor: 11.205

5.  Molecular mechanism of environmental d-xylose perception by a XylFII-LytS complex in bacteria.

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Journal:  Proc Natl Acad Sci U S A       Date:  2017-07-17       Impact factor: 11.205

6.  A scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid two-component system.

Authors:  Elisabeth C Lowe; Arnaud Baslé; Mirjam Czjzek; Susan J Firbank; David N Bolam
Journal:  Proc Natl Acad Sci U S A       Date:  2012-04-24       Impact factor: 11.205

7.  Mechanism of metal ion-induced activation of a two-component sensor kinase.

Authors:  Trisiani Affandi; Megan M McEvoy
Journal:  Biochem J       Date:  2019-01-15       Impact factor: 3.857

8.  Structural insight into the role of the PAS domainfor signal transduction in sensor-kinase BvgS.

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9.  Spontaneous Reversions of an Evolutionary Trait Loss Reveal Regulators of a Small RNA That Controls Multicellular Development in Myxobacteria.

Authors:  Yuen-Tsu N Yu; Manuel Kleiner; Gregory J Velicer
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10.  Transmembrane signaling in the sensor kinase DcuS of Escherichia coli: A long-range piston-type displacement of transmembrane helix 2.

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Journal:  Proc Natl Acad Sci U S A       Date:  2015-08-17       Impact factor: 11.205

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