Biological Insights from Structures of Two-Component Proteins

By R. Gao, Ann M Stock. Annual Review of Microbiology, 2009

790 citations recorded by the source corpus.

Two-component signal transduction based on phosphotransfer from a histidine protein kinase to a response regulator protein is a prevalent strategy for coupling environmental stimuli to adaptive responses in bacteria. In both histidine kinases and response regulators, modular domains with conserved structures and biochemical activities adopt different conformational states in the presence of stimuli or upon phosphorylation, enabling a diverse array of regulatory mechanisms based on inhibitory and/or activating protein-protein interactions imparted by different domain arrangements. This review summarizes some of the recent structural work that has provided insight to the functioning of bacterial histidine kinases and response regulators. Particular emphasis is placed on identifying features that are expected to be conserved among different two-component proteins from those that are expected to differ, with the goal of defining the extent to which knowledge of previously characterized two-component proteins can be applied to newly discovered systems.

Subfields: Ecology, Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/bd721c3e19d047f1928b8e5f75a7a6cf47f00ee5

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Citations in the corpus

Microbial Surface Colonization and Biofilm Development in Marine Environments (2015, background): “These responses lead to changes in cellular transcriptional, enzymatic, or mechanistic properties and alterations in microbial physiology and/or behavior (346, 349).”
Salmonella enterica Serovar Typhimurium Skills To Succeed in the Host: Virulence and Regulation (2013, background): “These regulators also contain an effector domain, which is often a DNA binding moiety activated upon phosphorylation to eventually alter gene transcription (250, 251).”
EcoCyc: a comprehensive database of Escherichia coli biology (2010, background): “Two-component systems couple the detection of environmental signals to regulatory responses based on a phosphotransfer reaction from a histidine protein kinase to a response regulator protein (9).”
High-resolution protein complexes from integrating genomic information with molecular simulation (2009, background): “Here, five individual kinases termed KinAKinE are known to phosphorylate the single domain RR Spo0F, which passes the phosphoryl group to Spo0B and finally to Spo0A, the terminal transcription factor/response regulator, which initiates sporulation (9, 10).”