scholarly journals Predicted Functional and Structural Diversity of Receiver Domains in Fungal Two-Component Regulatory Systems

mSphere ◽  
2021 ◽  
Author(s):  
Robert B. Bourret ◽  
Clay A. Foster ◽  
William E. Goldman
Keyword(s):  
Structural Diversity ◽  
Response Regulators ◽  
Histidine Kinases ◽  
Receiver Domain ◽  
Regulatory Systems ◽  
Two Component

Fungal two-component regulatory systems incorporate receiver domains into hybrid histidine kinases (HHKs) and response regulators. We constructed a nonredundant database of 670 fungal receiver domain sequences from 51 species sampled from nine fungal phyla.

Histidine kinases in signal transduction pathways of eukaryotes

1997 ◽  
Vol 110 (10) ◽  
pp. 1141-1145 ◽  
Author(s):  
W.F. Loomis ◽  
G. Shaulsky ◽  
N. Wang
Keyword(s):  
Signal Transduction ◽  
Response Regulator ◽  
Signal Transduction Pathways ◽  
Response Regulators ◽  
Histidine Kinases ◽  
Camp Phosphodiesterase ◽  
Wide Range ◽  
Two Component ◽  
Two Component Signal Transduction ◽  
Dependent Protein

Autophosphorylating histidine kinases are an ancient conserved family of enzymes that are found in eubacteria, archaebacteria and eukaryotes. They are activated by a wide range of extracellular signals and transfer phosphate moieties to aspartates found in response regulators. Recent studies have shown that such two-component signal transduction pathways mediate osmoregulation in Saccharomyces cerevisiae, Dictyostelium discoideum and Neurospora crassa. Moreover, they play pivotal roles in responses of Arabidopsis thaliana to ethylene and cytokinin. A transmembrane histidine kinase encoded by dhkA accumulates when Dictyostelium cells aggregate during development. Activation of DhkA results in the inhibition of its response regulator, RegA, which is a cAMP phosphodiesterase that regulates the cAMP dependent protein kinase PKA. When PKA is activated late in the differentiation of prespore cells, they encapsulate into spores. There is evidence that this two-component system participates in a feedback loop linked to PKA in prestalk cells such that the signal to initiate encapsulation is rapidly amplified. Such signal transduction pathways can be expected to be found in a variety of eukaryotic differentiations since they are rapidly reversible and can integrate disparate signals.

scholarly journals Cyanobacterial Two-Component Proteins: Structure,Diversity, Distribution, andEvolution

2006 ◽  
Vol 70 (2) ◽  
pp. 472-509 ◽  
Author(s):  
Mark K. Ashby ◽  
Jean Houmard
Keyword(s):  
Regulatory Mechanisms ◽  
Genome Plasticity ◽  
Cyanobacterial Genome ◽  
Response Regulators ◽  
Genome Sequences ◽  
Histidine Kinases ◽  
Physiological Properties ◽  
Two Component ◽  
Different Strains ◽  
Structure Diversity

SUMMARY A survey of the already characterized and potential two-component protein sequences that exist in the nine complete and seven partially annotated cyanobacterial genome sequences available (as of May 2005) showed that the cyanobacteria possess a much larger repertoire of such proteins than most other bacteria. By analysis of the domain structure of the 1,171 potential histidine kinases, response regulators, and hybrid kinases, many various arrangements of about thirty different modules could be distinguished. The number of two-component proteins is related in part to genome size but also to the variety of physiological properties and ecophysiologies of the different strains. Groups of orthologues were defined, only a few of which have representatives with known physiological functions. Based on comparisons with the proposed phylogenetic relationships between the strains, the orthology groups show that (i) a few genes, some of them clustered on the genome, have been conserved by all species, suggesting their very ancient origin and an essential role for the corresponding proteins, and (ii) duplications, fusions, gene losses, insertions, and deletions, as well as domain shuffling, occurred during evolution, leading to the extant repertoire. These mechanisms are put in perspective with the different genetic properties that cyanobacteria have to achieve genome plasticity. This review is designed to serve as a basis for orienting further research aimed at defining the most ancient regulatory mechanisms and understanding how evolution worked to select and keep the most appropriate systems for cyanobacteria to develop in the quite different environments that they have successfully colonized.

scholarly journals The Eukaryotic Two-Component Histidine Kinase Sln1p RegulatesOCH1via the Transcription Factor, Skn7p

2002 ◽  
Vol 13 (2) ◽  
pp. 412-424 ◽  
Author(s):  
Sheng Li ◽  
Susan Dean ◽  
Zhijian Li ◽  
Joe Horecka ◽  
Robert J. Deschenes ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Osmotic Stress ◽  
Binding Site ◽  
Histidine Kinase ◽  
Response Regulators ◽  
Hog Pathway ◽  
Receiver Domain ◽  
Osmotic Response ◽  
Two Component

The yeast “two-component” osmotic stress phosphorelay consists of the histidine kinase, Sln1p, the phosphorelay intermediate, Ypd1p and two response regulators, Ssk1p and Skn7p, whose activities are regulated by phosphorylation of a conserved aspartyl residue in the receiver domain. Dephospho-Ssk1p leads to activation of the hyper-osmotic response (HOG) pathway, whereas phospho-Skn7p presumably leads to activation of hypo-osmotic response genes. The multifunctional Skn7 protein is important in oxidative as well as osmotic stress; however, the Skn7p receiver domain aspartate that is the phosphoacceptor in the SLN1 pathway is dispensable for oxidative stress. Like many well-characterized bacterial response regulators, Skn7p is a transcription factor. In this report we investigate the role of Skn7p in osmotic response gene activation. Our studies reveal that the Skn7p HSF-like DNA binding domain interacts with acis-acting element identified upstream ofOCH1 that is distinct from the previously defined HSE-like Skn7p binding site. Our data support a model in which Skn7p receiver domain phosphorylation affects transcriptional activation rather than DNA binding to this class of DNA binding site.

scholarly journals Blue Light Regulated Two-Component Systems: Enzymatic and Functional Analyses of Light-Oxygen-Voltage (LOV)-Histidine Kinases and Downstream Response Regulators

Biochemistry ◽  
2013 ◽  
Vol 52 (27) ◽  
pp. 4656-4666 ◽  
Author(s):  
Fernando Correa ◽  
Wen-Huang Ko ◽  
Victor Ocasio ◽  
Roberto A. Bogomolni ◽  
Kevin H. Gardner
Keyword(s):  
Blue Light ◽  
Response Regulators ◽  
Histidine Kinases ◽  
Component Systems ◽  
Two Component ◽  
Two Component Systems ◽  
Functional Analyses

Histidine kinases from bacteria to humans

2013 ◽  
Vol 41 (4) ◽  
pp. 1023-1028 ◽  
Author(s):  
Paul V. Attwood
Keyword(s):  
Histidine Kinase ◽  
Tyrosine Kinases ◽  
Mitochondrial Enzymes ◽  
Response Regulators ◽  
Histidine Kinases ◽  
Two Component ◽  
Higher Eukaryotes ◽  
Histidine Phosphorylation ◽  
Eukaryotic Organisms ◽  
Nucleoside Diphosphate Kinases

It is more than 50 years since protein histidine phosphorylation was first discovered in 1962 by Boyer and co-workers; however, histidine kinases are still much less well recognized than the serine/threonine and tyrosine kinases. The best-known histidine kinases are the two-component signalling kinases that occur in bacteria, fungi and plants. The mechanisms and functions of these kinases, their cognate response regulators and associated phosphorelay proteins are becoming increasingly well understood. When genomes of higher eukaryotes began to be sequenced, it did not appear that they contained two-component histidine kinase system homologues, apart from a couple of related mitochondrial enzymes that were later shown not to function as histidine kinases. However, as a result of the burgeoning sequencing of genomes from a wide variety of eukaryotic organisms, it is clear that there are proteins that correspond to components of the two-component histidine kinase systems in higher eukaryotes and that operational two-component kinase systems are likely to occur in these organisms. There is unequivocal direct evidence that protein histidine phosphorylation does occur in mammals. So far, only nucleoside diphosphate kinases have been shown to be involved in protein histidine phosphorylation, but their mechanisms of action are not well understood. It is clear that other, yet to be identified, histidine kinases also exist in mammals and that protein histidine phosphorylation may play important roles in higher eukaryotes.

Redox signalling in chloroplasts and mitochondria: genomic and biochemical evidence for two-component regulatory systems in bioenergetic organelles

2001 ◽  
Vol 29 (4) ◽  
pp. 403-407 ◽  
Author(s):  
J. Forsberg ◽  
M. Rosenquist ◽  
L. Fraysse ◽  
J. F. Allen
Keyword(s):  
Eukaryotic Cell ◽  
Response Regulators ◽  
Redox Signalling ◽  
Organellar Genomes ◽  
Regulatory Systems ◽  
Two Component ◽  
Sensor Kinases ◽  
Photosynthesis And Respiration ◽  
Sequence Similarities

Redox chemistry is central to the primary functions of chloroplasts and mitochondria, that is, to energy conversion in photosynthesis and respiration. However, these bioenergetic organelles always contain very small, specialized genetic systems, relics of their bacterial origin. At huge cost, organellar genomes contain, typically, a mere 0.1 % of the genetic information in a eukaryotic cell. There is evidence that chloroplast and mitochondrial genomes encode proteins whose function and biogenesis are particularly tightly governed by electron transfer. We have identified nuclear genes for ‘bacterial’ histidine sensor kinases and aspartate response regulators that seem to be targeted to chloroplast and mitochondrial membranes. Sequence similarities to cyano-bacterial redox signalling components indicate homology and suggest conserved sensory and signalling functions. Two-component redox signalling pathways might be ancient, conserved mechanisms that permit endogenous control over the biogenesis, in situ, of bioenergetic complexes of chloroplasts and mitochondria.

scholarly journals Autophosphorylation and Dephosphorylation by Soluble Forms of the Nitrate-Responsive Sensors NarX and NarQ from Escherichia coli K-12

2008 ◽  
Vol 190 (11) ◽  
pp. 3869-3876 ◽  
Author(s):  
Chris E. Noriega ◽  
Radomir Schmidt ◽  
Michael J. Gray ◽  
Li-Ling Chen ◽  
Valley Stewart
Keyword(s):  
Escherichia Coli ◽  
Rate Constant ◽  
Response Regulator ◽  
Response Regulators ◽  
Amino Terminal ◽  
Regulatory Systems ◽  
Two Component ◽  
Nitrite Nitrate ◽  
Nitrate And Nitrite ◽  
K 12

ABSTRACT NarX-NarL and NarQ-NarP are paralogous two-component regulatory systems that control Escherichia coli gene expression in response to the respiratory oxidants nitrate and nitrite. Nitrate stimulates the autophosphorylation rates of the NarX and NarQ sensors, which then phosphorylate the response regulators NarL and NarP to activate and repress target operon transcription. Here, we investigated both the autophosphorylation and dephosphorylation of soluble sensors in which the maltose binding protein (MBP) has replaced the amino-terminal transmembrane sensory domain. The apparent affinities (Km ) for ADP were similar for both proteins, about 2 μM, whereas the affinity of MBP-NarQ for ATP was lower, about 23 μM. At a saturating concentration of ATP, the rate constant of MBP-NarX autophosphorylation (about 0.5 × 10−4 s−1) was lower than that observed for MBP-NarQ (about 2.2 × 10−4 s−1). At a saturating concentration of ADP, the rate constant of dephosphorylation was higher than that of autophosphorylation, about 0.03 s−1 for MBP-NarX and about 0.01 s−1 for MBP-NarQ. For other studied sensors, the published affinities for ADP range from about 16 μM (KinA) to about 40 μM (NtrB). This suggests that only a small proportion of NarX and NarQ remain phosphorylated in the absence of nitrate, resulting in efficient response regulator dephosphorylation by the remaining unphosphorylated sensors.

scholarly journals VpsR, a Member of the Response Regulators of the Two-Component Regulatory Systems, Is Required for Expression ofvps Biosynthesis Genes and EPSETr-Associated Phenotypes in Vibrio cholerae O1 El Tor

2001 ◽  
Vol 183 (5) ◽  
pp. 1716-1726 ◽  
Author(s):  
Fitnat H. Yildiz ◽  
Nadia A. Dolganov ◽  
Gary K. Schoolnik
Keyword(s):  
Vibrio Cholerae ◽  
Biofilm Formation ◽  
Genetic Background ◽  
Bactericidal Action ◽  
Response Regulators ◽  
Targeted Disruption ◽  
Regulatory Systems ◽  
Two Component ◽  
Vibrio Cholerae O1 ◽  
El Tor

ABSTRACT The rugose colonial variant of Vibrio cholerae O1 El Tor produces an exopolysaccharide (EPSETr) that enables the organism to form a biofilm and to resist oxidative stress and the bactericidal action of chlorine. Transposon mutagenesis of the rugose variant led to the identification of vpsR, which codes for a homologue of the NtrC subclass of response regulators. Targeted disruption of vpsR in the rugose colony genetic background yielded a nonreverting smooth-colony morphotype that produced no detectable EPSETr and did not form an architecturally mature biofilm. Analysis of two genes, vpsA andvpsL, within the vps cluster of EPSETr biosynthesis genes revealed that their expression is induced above basal levels in the rugose variant, compared to the smooth colonial variant, and requires vpsR. These results show that VpsR functions as a positive regulator of vpsAand vpsL and thus acts to positively regulate EPSETr production and biofilm formation.

scholarly journals New Insights into Multistep-Phosphorelay (MSP)/Two-Component System (TCS) Regulation: Are Plants and Bacteria That Different?

Plants ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 590 ◽  
Author(s):  
Virtudes Mira-Rodado
Keyword(s):  
Signal Transduction ◽  
Arabidopsis Thaliana ◽  
Model Organism ◽  
Response Regulators ◽  
Two Component System ◽  
Histidine Kinases ◽  
Signaling Mechanism ◽  
Component System ◽  
Two Component ◽  
Different Types

The Arabidopsis multistep-phosphorelay (MSP) is a signaling mechanism based on a phosphorelay that involves three different types of proteins: Histidine kinases, phosphotransfer proteins, and response regulators. Its bacterial equivalent, the two-component system (TCS), is the most predominant device for signal transduction in prokaryotes. The TCS has been extensively studied and is thus generally well-understood. In contrast, the MSP in plants was first described in 1993. Although great advances have been made, MSP is far from being completely comprehended. Focusing on the model organism Arabidopsis thaliana, this review summarized recent studies that have revealed many similarities with bacterial TCSs regarding how TCS/MSP signaling is regulated by protein phosphorylation and dephosphorylation, protein degradation, and dimerization. Thus, comparison with better-understood bacterial systems might be relevant for an improved study of the Arabidopsis MSP.

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