Histidine kinases: diversity of domain organization

Dutta, Rinku; Qin, Ling; Inouye, Masayori

doi:10.1046/j.1365-2958.1999.01646.x

Cited by 243 publications

(206 citation statements)

References 49 publications

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“…Comparing the shared elements of TH-CikA, TH-CikA*, TH-CikA∆N and TH-CikA∆G, we hypothesized that either HPK or PsR is required for the interaction that leads to arrhythmia upon overexpression. HPK domains are known to form homodimers through a specific subdomain, which is also the platform for interaction with its cognate RR (Dutta et al, 1999). Furthermore, we confirmed that active CikA is a dimer in solution (Fig.…”

Section: Overexpression Of Psr-containing Cika Variants Causes Arrhytsupporting

confidence: 75%

“…Bioinformatics analysis showed the HPK domain of CikA to be related to the class I histidine kinases as exemplified by EnvZ, whose structure has been partially determined (Dutta et al, 1999). Thus, the C-terminal portion of dimeric CikA (Fig.…”

Section: Model For Function Of Cikamentioning

confidence: 99%

“…A and B. Representation of structure of EnvZ (A, adapted from Dutta et al, 1999) and inferred structure of CikA (B). For EnvZ, only the cytoplasmic catalytic region is represented.…”

Section: Model For Function Of Cikamentioning

confidence: 99%

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The pseudo‐receiver domain of CikA regulates the cyanobacterial circadian input pathway

Zhang

Dong

Golden

2006

Molecular Microbiology

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SummaryCikA (circadian input kinase) is a component of the cyanobacterial circadian clock that aids in synchronizing the endogenous oscillator with the external environment. cikA mutants of the prokaryotic circadian model organism Synechococcus elongatus PCC 7942 fail to reset the phase of the circadian rhythm of gene expression after an environmental time cue, and also exhibit reduced amplitude and shortened period of circadian oscillation. CikA has histidine protein kinase (HPK) activity that is modulated in vitro by GAF and pseudo -receiver (PsR) domains. Here we show that the PsR domain negatively regulates HPK activity in vivo and also serves as an interaction module to dock CikA at a specific subcellular location. Phenotypes conferred by alleles that encode CikA variants showed that all domains except the featureless Nterminus are required for CikA function. Overexpression of all alleles that encode the PsR domain, whether or not the HPK is functional, caused a dominant arrhythmic phenotype, whereas overexpressed variants that lack PsR did not. Subcellular localization of intact CikA identified a polar focus whereas a variant without PsR showed uniform distribution in the cell, consistent with a model in which PsR mediates interaction with other input pathway components.

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Section: Overexpression Of Psr-containing Cika Variants Causes Arrhytsupporting

confidence: 75%

Section: Model For Function Of Cikamentioning

confidence: 99%

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The pseudo‐receiver domain of CikA regulates the cyanobacterial circadian input pathway

Zhang

Dong

Golden

2006

Molecular Microbiology

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“…In summary, the phosphate is passed from the DD to the receiver domain of the RR. The only known exception is the chemotactic two-component system, where the phosphate is passed, not from the DD, but from a histidinecontaining phosphotransfer domain, to the receiver domain of the RR (10). Therefore, in this work, we have eliminated the chemotactic proteins, and we will refer to the receiver domain of a RR protein simply as ''RR.…”

mentioning

confidence: 99%

Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases

Shakhnovich

Mirny

2003

Proc. Natl. Acad. Sci. U.S.A.

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The binding between a PK and its target is highly specific, despite the fact that many different PKs exhibit significant sequence and structure homology. There must be, then, specificity-determining residues (SDRs) that enable different PKs to recognize their unique substrate. Here we use and further develop a computational procedure to discover putative SDRs (PSDRs) in protein families, whereby a family of homologous proteins is split into orthologous proteins, which are assumed to have the same specificity, and paralogous proteins, which have different specificities. We reason that PSDRs must be similar among orthologs, whereas they must necessarily be different among paralogs. Our statistical procedure and evolutionary model identifies such residues by discriminating a functional signal from a phylogenetic one. As case studies we investigate the prokaryotic two-component system and the eukaryotic AGC (i.e., cAMP-dependent PK, cGMP-dependent PK, and PKC) PKs. Without using experimental data, we predict PSDRs in prokaryotic and eukaryotic PKs, and suggest precise mutations that may convert the specificity of one PK to another. We compare our predictions with current experimental results and obtain considerable agreement with them. Our analysis unifies much of existing data on PK specificity. Finally, we find PSDRs that are outside the active site. Based on our results, as well as structural and biochemical characterizations of eukaryotic PKs, we propose the testable hypothesis of ''specificity via differential activation'' as a way for the cell to control kinase specificity.

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“…The residues Cys 170 /Phe 175 was found to be crucial in the CqsSvc as it signifies the ligand chain length [44]. The CqsSvc Sensor histidine kinases has a N-terminal transmembrane sensing domains, dimerization histidine phosphotransfer (DHp) domains and C-terminal catalytic ATPbinding (CA) domains [48]. It has been theoretically defined to have two-state model for histidine kinases with a ''kinase on'' and a ''kinase off'' mechanism [49].…”

Section: Cqssmentioning

confidence: 99%

Meddling Vibrio cholerae Murmurs: A Neoteric Advancement in Cholera Research

2015

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Cholera, a known diarrheal disease is associated with various risk factors like hypovolemic shock, rice watery stools, and death in developing countries. The overuse of antibiotics to treat cholera imposed a selective pressure for the emergence and spread of multi-drug resistant Vibrio cholerae strains. The failure of conventional antimicrobial therapy urged the researchers to find an alternative therapy that could meddle the cholera murmurs (Quorum Sensing). It seems to effectively overcome the conventional cholera therapies in parallel to decrease the morbidity and mortality rate in the developing countries. The paramount objective of this review essentially focuses on the different Quorum Sensing (QS) regulatory switches governing virulence and pathogenicity of Vibrio cholerae. This review also provides an insight into the plausible QS targets that could be exploited to bring about a breakthrough to the prevailing cholera therapy.

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Histidine kinases: diversity of domain organization

Cited by 243 publications

References 49 publications

The pseudo‐receiver domain of CikA regulates the cyanobacterial circadian input pathway

The pseudo‐receiver domain of CikA regulates the cyanobacterial circadian input pathway

Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases

Meddling Vibrio cholerae Murmurs: A Neoteric Advancement in Cholera Research

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