Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.13.3 (histidine kinase)
 2,405 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two-component regulatory systems require highly specific interactions between histidine kinase (transmitter) and response regulator (receiver) proteins. We have developed a novel genetic strategy that is based on tightly regulated synthesis of a given protein to identify domains and residues of an interacting protein that are critical for interactions between them. Using a reporter strain synthesizing the nonpartner kinase VanS under tight arabinose control and carrying a promoter-lacZ fusion activated by phospho-PhoB, we isolated altered recognition (AR) mutants of PhoB showing enhanced activation (phosphorylation) by VanS as arabinose-dependent Lac+ mutants. Changes in the PhoBAR mutants cluster in a "patch" near the proposed helix 4 of PhoB based on the CheY crystal structure (a homolog of the PhoB receiver domain) providing further evidence that helix 4 lies in the kinase-regulator interface. Based on the CheY structure, one mutant has an additional change in a region that may propagate a conformational change to helix 4. The overall genetic strategy described here may also be useful for studying interactions of other components of the vancomycin resistance and P1 signal transduction pathways, other two-component regulatory systems, and other interacting proteins. Conditionally replicative oriRR6K gamma attP "genome targeting" suicide plasmids carrying mutagenized phoB coding regions were integrated into the chromosome of a reporter strain to create mutant libraries; plasmids encoding mutant PhoB proteins were subsequently retrieved by P1-Int-Xis cloning. Finally, the use of similar genome targeting plasmids and P1-Int-Xis cloning should be generally useful for constructing genomic libraries from a wide array of organisms.
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PMID:Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions. 896 56

Both regulated expression of the clock genes kaiA, kaiB, and kaiC and interactions among the Kai proteins are proposed to be important for circadian function in the cyanobacterium Synechococcus sp. strain PCC 7942. We have identified the histidine kinase SasA as a KaiC-interacting protein. SasA contains a KaiB-like sensory domain, which appears sufficient for interaction with KaiC. Disruption of the sasA gene lowered kaiBC expression and dramatically reduced amplitude of the kai expression rhythms while shortening the period. Accordingly, sasA disruption attenuated circadian expression patterns of all tested genes, some of which became arrhythmic. Continuous sasA overexpression eliminated circadian rhythms, whereas temporal overexpression changed the phase of kaiBC expression rhythm. Thus, SasA is a close associate of the cyanobacterial clock that is necessary to sustain robust circadian rhythms.
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PMID:A kaiC-interacting sensory histidine kinase, SasA, necessary to sustain robust circadian oscillation in cyanobacteria. 1078 37

Cyanobacteria respond to nutrient stress conditions by degrading their light-harvesting complexes for photosynthesis, a process regulated in Synechococcus sp. PCC 7942 by the sensor histidine kinase non-bleaching sensor (NblS). In yeast two-hybrid screenings for proteins interacting with NblS we have identified a novel type of protein, named SipA for NblS interacting protein A. Specific binding between NblS and SipA is observed with both yeast and bacterial two-hybrid systems. Additional yeast two-hybrid screenings with SipA as bait further confirmed the specificity of the interaction and allowed us to map their determinants to the ATP-binding domain of NblS. Strong conservation and coevolution of both NblS and SipA in cyanobacteria further suggests the importance of SipA in the context of the NblS signal transduction network.
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PMID:SipA, a novel type of protein from Synechococcus sp. PCC 7942, binds to the kinase domain of NblS. 1645 Nov 77

The actin cytoskeleton of the yeast Saccharomyces cerevisiae can be altered rapidly in response to external cues. We reported previously that S. cerevisiae responds to low-pH stress by transiently depolarizing its actin cytoskeleton, and that this step requires a mitogen-activated protein kinase, high osmolarity glycerol 1 (Hog1p). This study further investigated the components involved in this actin reorganization at pH 3.0. Gene deletions on the Sln1p branch of the HOG pathway completely blocked actin depolarization, suggesting that Hog1p activation depends mainly on the osmosensor Sln1p. The protein-synthesis inhibitor cycloheximide did not influence the time course of actin depolarization, suggesting that the depolarization is a direct effect of the HOG pathway. Deletion of the scaffolding protein, Spa2p, or the Spa2p-interacting protein Pea2p, markedly inhibited the depolarization, and further deletion of the formin protein, Bni1p, notably delayed actin repolarization. Our results suggest the involvement of polarisome proteins, such as Spa2p, Pea2p and Bni1p, but not Bud6p, in Hog1p-dependent reorganization of the yeast actin cytoskeleton at low pH.
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PMID:Importance of polarisome proteins in reorganization of actin cytoskeleton at low pH in Saccharomyces cerevisiae. 1963 59

Cyanobacteria have developed a light-harvesting antenna complex known as the phycobilisome. When cells are starved for nutrients or exposed to high light, the phycobilisome is rapidly degraded (bleaching). It has been suggested that in the cyanobacterium Synechococcus elongatus PCC 7942, the bleaching process is regulated by a two-component histidine kinase, NblS. To clarify the signaling pathway involving NblS, we identified the NblS-interacting response regulators RpaB and SrrA. In vitro assays using recombinant proteins showed that both RpaB and SrrA can receive phosphoryl groups from autophosphorylated NblS; the NblS-interacting protein SipA clearly enhances the phosphotransfer activity from NblS to RpaB and SrrA. In addition, NblS prefers SrrA over RpaB as the phosphotransfer target with or without SipA. Gel mobility shift assay revealed that both RpaB and SrrA can bind to the upstream region of nblA, a major regulatory factor in the bleaching process. nblA transcript accumulates in nblS or rpaB mutants even under normal growth conditions, while in the srrA disruptant the nblA transcripts are slightly up-regulated under stress conditions. These observations suggest that the bleaching signal transduction pathway via NblS is regulated by RpaB and that SrrA is partially involved.
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PMID:Interactions between histidine kinase NblS and the response regulators RpaB and SrrA are involved in the bleaching process of the cyanobacterium Synechococcus elongatus PCC 7942. 2202 5

Ethylene is a gaseous hormone that regulates many processes involved in plant growth, development and stress responses. Previously, we found that the tobacco ethylene receptor NTHK1 (Nicotiana tabacum histidine kinase 1) promotes seedling growth and affects plant salt stress responses. In this study, NTHK1 ethylene receptor-interacting protein 2 (NEIP2) was identified and further characterized in relation to these processes. NEIP2 contains three ankyrin repeats that mediate an interaction with NTHK1 as demonstrated by yeast two-hybrid, glutathione S-transferase (GST) pull-down and co-immunoprecipitation assays. NTHK1 phosphorylates NEIP2 in vitro. Salt stress and ethylene treatment induce NEIP2 accumulation in the first few hours and then the NEIP2 can be phosphorylated in planta. The overexpression of NTHK1 enhances NEIP2 accumulation in the presence of ethylene and salt stress. NEIP2 overexpression promotes plant growth but reduces ethylene responses, which is consistent with the functions of NTHK1. Additionally, NEIP2 improves plant performance under salt and oxidative stress. These results suggest that ethylene-induced NEIP2 probably acts as a brake to reduce ethylene response but resumes growth through interaction with NTHK1. Manipulation of NEIP2 may be beneficial for crop improvement.
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PMID:Tobacco ankyrin protein NEIP2 interacts with ethylene receptor NTHK1 and regulates plant growth and stress responses. 2563 61

The redox state of the photosynthetic electron transport chain is known to act as a signal to regulate the transcription of key genes involved in the acclimation responses to environmental changes. We hypothesized that the protein thioredoxin (Trx) acts as a mediator connecting the redox state of the photosynthetic electron transport chain and transcriptional regulation, and established a screening system to identify transcription factors (TFs) that interact with Trx. His-tagged TFs and S-tagged mutated form of Trx, TrxMC35S, whose active site cysteine 35 was substituted with serine to trap the target interacting protein, were co-expressed in E. coli cells and Trx-TF complexes were detected by immuno-blotting analysis. We examined the interaction between Trx and ten OmpR family TFs encoded in the chromosome of the cyanobacterium Synechocystis sp. PCC 6803 (S.6803). Although there is a highly conserved cysteine residue in the receiver domain of all OmpR family TFs, only three, RpaA (Slr0115), RpaB (Slr0947) and ManR (Slr1837), were identified as putative Trx targets [corrected].The recombinant forms of wild-type TrxM, RpaA, RpaB and ManR proteins from S.6803 were purified following over-expression in E. coli and their interaction was further assessed by monitoring changes in the number of cysteine residues with free thiol groups. An increase in the number of free thiols was observed after incubation of the oxidized TFs with Trx, indicating the reduction of cysteine residues as a consequence of interaction with Trx. Our results suggest, for the first time, the possible regulation of OmpR family TFs through the supply of reducing equivalents from Trx, as well as through the phospho-transfer from its cognate sensor histidine kinase.
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PMID:Identification of OmpR-family response regulators interacting with thioredoxin in the Cyanobacterium Synechocystis sp. PCC 6803. 2587 89