An Escherichia coli protein that exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His‐Asp phosphorelay

  title={An Escherichia coli protein that exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His‐Asp phosphorelay},
  author={Tomoaki Ogino and Masahiro Matsubara and Naoki Kato and Yoshihiro Nakamura and Takeshi Mizuno},
  journal={Molecular Microbiology},
The Escherichia coli sensory kinase, ArcB, possesses a histidine‐containing phosphotransfer (HPt) domain, which is implicated in the His‐Asp multistep phosphorelay. We searched for a presumed phosphohistidine phosphatase, if present, which affects the function of the HPt domain through its dephosphorylation activity. Using in vivo screening, we first identified a gene that appeared to interfere with the His‐Asp phosphorelay between the HPt domain and the receiver domain of OmpR, provided that… 

Crystal structure of the protein histidine phosphatase SixA in the multistep His‐Asp phosphorelay

The results provide the first three‐dimensional view of a bacterial protein histidine phosphatase, revealing a compact α/β architecture related to a family of phosphatases containing the arginine‐histidine‐glycine (RHG) motif at their active sites.

Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay.

SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity and preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P212121, having one molecule in the crystallographic asymmetric unit.

Functional Characterization of the Receiver Domain for Phosphorelay Control in Hybrid Sensor Kinases

In vitro assays confirmed the existence of a similar hyperphosphorylation reaction in the HK domain of the EvgS mutant in which the Asp residue was replaced with Ala, confirming the validity of the control mechanism proposed from profiling of phosphorylation in vitro.

Structural and functional characterization of the c-terminal domain of the ecdysteroid phosphate phosphatase from bombyx mori reveals a new enzymatic activity.

The crystal structure of the ecdysone phosphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain is presented, the first structure of a steroid phosphate phosph atase, and it is suggested that EPPase and its closest homologues can be grouped into a distinct subfamily in the large 2H-phosphatase superfamily of proteins.

Phosphorylation of the Spo0B Response Regulator Phosphotransferase of the Phosphorelay Initiating Development inBacillus subtilis *

The His30 of Spo0B resides in a domain with little sequence homology to functionally equivalent domains in the phosphorelays of other bacterial and yeast systems, suggesting that the two types of phosphotransfer domains evolved convergently.

A novel feature of the multistep phosphorelay in Escherichia coli: a revised model of the RcsC → YojN → RcsB signalling pathway implicated in capsular synthesis and swarming behaviour

Several lines of in vivo and in vitro evidence are provided that a novel and unique His‐containing phosphotransmitter (named YojN) is essential for this signalling system that is involved in the regulation of capsular polysaccharide synthesis in Escherichia coli.

Protein Phosphohistidine Phosphatases of the HP Superfamily.

  • D. Rigden
  • Biology
    Methods in molecular biology
  • 2020
The recently characterized eukaryotic PHPP PGAM5 only has one currently known substrate, NDPK-B, through which it helps regulate T-cell signaling, suggesting that PHPP activity has arisen independently in different lineages of the HP superfamily.



Phosphotransfer circuitry of the putative multi‐signal transducer, ArcB, of Escherichia coli: in vitro studies with mutants

Evidence obtained in vitro supports the view that ArcB can serve as a powerful device for not only propagating multi‐signals, but also making up signalling networks, in ways more sophisticated than previously thought.

In vitro phosphorylation study of the arc two-component signal transduction system of Escherichia coli

Data are consistent with a signal transduction model in which reception of a membrane signal triggers autophosphorylation of H1 at His292 and ArcA receives the phosphoryl group from either His292 or His717, the relative contribution of which is regulated by cytosolic effectors.

A novel device of bacterial signal transducers.

It is suggested that this unique feature of ArcB and BarA, in terms of the signaling modules, make it possible for these sensory kinases to function as dual‐signaling transducers.

Multisensory activation of the phosphorelay initiating sporulation in Bacillus subtilis: identification and sequence of the protein kinase of the alternate pathway

Although double mutants kinA kinB cannot sporulate and assume a stage 0 phenotype, the SpoA∼P‐dependent regulation of the abrB gene is normal in these strains, suggesting that low levels of SpoA ∼P accumulate even in the absence of both kinases.

Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli.

  • T. Mizuno
  • Biology
    DNA research : an international journal for rapid publication of reports on genes and genomes
  • 1997
The recently determined entire genomic sequence of Escherichia coli allowed us to compile systematically a complete list of genes encoding such two- component signal transduction proteins, and revealed that at least 62 open reading frames (ORFs) were identified as putative members of the two-component signal transducers in this single species.

A novel sensor‐regulator protein that belongs to the homologous family of signal‐transduction proteins involved in adaptive responses in Escherichia coli

The protein identified in this study is probably a novel member of the homologous family of proteins involved in bacterial adaptive responses and was designated as barA (bacterial adaptive responses) and mapped at 60 min on the E. coli genetic map.

Integration of multiple domains in a two‐component sensor protein: the Bordetella pertussis BvgAS phosphorelay.

It is demonstrated that phosphorylated, purified C‐terminal domain alone is sufficient for phosphotransfer to BvgA, and an obligatory role for an alternate phosphodonor module in the BvgAS phosphorelay is indicated.

Hyphal development in Neurospora crassa: involvement of a two-component histidine kinase.

Evidence is found for the existence of two-component histidine kinases in the eukaryotic filamentous fungus Neurospora crassa based on screening with degenerate primers to conserved regions of these signaling proteins and subsequent cloning and sequencing of one member of this newly discovered group shows that the predicted protein sequence shares homology with both the kinase and response regulator modules of three-component signaling proteins.

The arcB gene of Escherichia coli encodes a sensor‐regulator protein for anaerobic repression of the arc modulon

It is shown that ArcB is a membrane sensor protein on the basis of its deduced amino acid sequence (778 residues), hydropathicity profile, and cellular distribution.