ArticleThe Biochemical journal2001
HstK, a cyanobacterial protein with both a serine/threonine kinase domain and a histidine kinase domain: implication for the mechanism of signal transduction.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Comprehensive Phosphoproteomic Analysis ofACS omega · 2021Article
- Tracing the origin and evolution of pseudokinases across the tree of life.Science signaling · 2019Article
- Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.PloS one · 2011Article
- Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis.The Journal of biological chemistry · 2010Article
- Genomic structure of an economically important cyanobacterium, Arthrospira (Spirulina) platensis NIES-39.DNA research : an international journal for rapid publication of reports on genes and genomes · 2010Article
- Cyanobacterial heterocysts.Cold Spring Harbor perspectives in biology · 2010Review
- Genome-wide survey of putative serine/threonine protein kinases in cyanobacteria.BMC genomics · 2007Article
- Two genes encoding protein kinases of the HstK family are involved in synthesis of the minor heterocyst-specific glycolipid in the cyanobacterium Anabaena sp. strain PCC 7120.Journal of bacteriology · 2007Article
- A pair of iron-responsive genes encoding protein kinases with a Ser/Thr kinase domain and a His kinase domain are regulated by NtcA in the Cyanobacterium Anabaena sp. strain PCC 7120.Journal of bacteriology · 2006Article
- Cyanobacterial two-component proteins: structure, diversity, distribution, and evolution.Microbiology and molecular biology reviews : MMBR · 2006Review
- Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes.BMC genomics · 2005Article
- Identification of two-component regulatory systems in Bifidobacterium infantis by functional complementation and degenerate PCR approaches.Applied and environmental microbiology · 2003Article
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3 authors.
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Abstract
Two distinct families of protein kinases are involved in signal transduction: Ser, Thr and Tyr kinases, which are predominantly found among eukaryotes, and His kinases, as part of bacterial two-component signalling systems. Genetic studies in Arabidopsis and Saccharomyces have demonstrated that bacterial-type two-component systems may act upstream of Ser/Thr kinases in the same signalling pathway, but how this coupling is accomplished remains unclear. In the present study, we report the characterization of a protein kinase, HstK, from the N(2)-fixing cyanobacterium Anabaena sp. PCC 7120, that possesses both a Ser/Thr kinase domain and a His kinase domain. Proteins with a structural architecture similar to that of HstK can be found in the eukaryote, Schizosaccharomyces pombe, and the bacterium, Rhodococcus sp. M5. HstK was present in cells grown with NH(4)(+) or N(2) as the nitrogen source, but was absent in cells grown with NO(3)(-). The hstK gene was inactivated and the mutant phenotype was characterized. The catalytic domain of the Ser/Thr kinase of HstK functionally replaced that of Hog1p, a well-characterized protein kinase required for the response to high osmolarity in the S. cerevisiae heterologous system. The unusual multidomain structure of HstK suggests that a two-component system could be directly coupled to Ser/Thr kinases in the same signal transduction pathway.
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