Phosphorelay of non-orthodox two component systems functions through a bi-molecular mechanism in vivo: the case of ArcB
Author:
Affiliation:
1. Department of Life Sciences
2. Imperial College London
3. UK
4. Centre for Integrative Systems Biology and Bioinformatics
5. Department of Mathematics
6. University of Copenhagen
7. Denmark
Abstract
Two-component systems play a central part in bacterial signal transduction.
Funder
Human Frontier Science Program
Biotechnology and Biological Sciences Research Council
Publisher
Royal Society of Chemistry (RSC)
Subject
Molecular Biology,Biotechnology
Link
http://pubs.rsc.org/en/content/articlepdf/2015/MB/C4MB00720D
Reference45 articles.
1. Two-Component Signal Transduction
2. Biological Insights from Structures of Two-Component Proteins
3. The mechanism of signal transduction by two-component systems
4. Evolution of Two-Component Signal Transduction Systems
5. Structural Characterization of the Predominant Family of Histidine Kinase Sensor Domains
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1. Energy dependence of signalling dynamics and robustness in bacterial two component systems;2023-02-12
2. Maximization of information transmission influences selection of native phosphorelay architectures;PeerJ;2021-06-10
3. What influences selection of native phosphorelay architectures?;2020-05-26
4. Routes of phosphoryl group transfer during signal transmission and signal decay in the dimeric sensor histidine kinase ArcB;Journal of Biological Chemistry;2018-08
5. General Aspects of Two-Component Regulatory Circuits in Bacteria: Domains, Signals and Roles;Current Protein & Peptide Science;2017-08-16
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