ArticleJournal of bacteriology2009
In vivo domain-based functional analysis of the major sporulation sensor kinase, KinA, in Bacillus subtilis.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- Modulation of the Sporulation Dynamics in the Plant-Probiotic Bacillus velezensis 83 via Carbon and Quorum-Sensing Metabolites.Probiotics and antimicrobial proteins · 2025Article
- Conservation of sporulation genes and a transmembrane-containing Spo0B variant inbioRxiv : the preprint server for biology · 2025Article
- Arabinose Plays an Important Role in Regulating the Growth and Sporulation ofInternational journal of molecular sciences · 2023Article
- Three Orphan Histidine Kinases Inhibit Clostridioides difficile Sporulation.Journal of bacteriology · 2022Article
- Article
- Artificial Sporulation Induction (ASI) byInternational journal of molecular sciences · 2020Article
- An EngineeredACS synthetic biology · 2019Article
- Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria.Frontiers in microbiology · 2019Article
- Integration of cell cycle signals by multi-PAS domain kinases.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The PAS domains of the major sporulation kinase in Bacillus subtilis play a role in tetramer formation that is essential for the autokinase activity.MicrobiologyOpen · 2017Article
- Multimerization of the Virulence-Enhancing Group A Streptococcus Transcription Factor RivR Is Required for Regulatory Activity.Journal of bacteriology · 2017Article
- Slowdown of growth controls cellular differentiation.Molecular systems biology · 2016Article
- Salt-sensitivity of σ(H) and Spo0A prevents sporulation of Bacillus subtilis at high osmolarity avoiding death during cellular differentiation.Molecular microbiology · 2016Article
- Time Series Analysis of theFrontiers in microbiology · 2016Article
- Evidence that Autophosphorylation of the Major Sporulation Kinase in Bacillus subtilis Is Able To Occur in trans.Journal of bacteriology · 2015Article
- Computational modelling and analysis of the molecular network regulating sporulation initiation in Bacillus subtilis.BMC systems biology · 2014Article
- Asymmetric division and differential gene expression during a bacterial developmental program requires DivIVA.PLoS genetics · 2014Article
- Role of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA.Journal of bacteriology · 2013Article
- Ultrasensitivity of the Bacillus subtilis sporulation decision.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sensor histidine kinases are widely used by bacteria to detect and respond to environmental signals. In Bacillus subtilis, KinA is a major kinase providing phosphate input to the phosphorelay that activates the sporulation pathway upon starvation via the phosphorylated Spo0A transcription factor. KinA contains three PAS domains in its amino-terminal sensor domain, which appear to be involved in the sensing of an unidentified sporulation signal(s) produced upon starvation. Prior biochemical studies have suggested that KinA forms a homodimer as a functional enzyme and that the most amino-terminal PAS domain (PAS-A) plays an important role in sensing the signal(s) to activate an ATP-dependent autophosphorylation reaction to a histidine residue. To analyze the structure and function of the kinase in vivo, we have used a strain in which the synthesis of KinA is under the control of an isopropyl-beta-d-thiogalactopyranoside (IPTG)-inducible promoter. In vivo functional studies in combination with domain-based deletion analysis show that the cytosolic KinA forms a homo-oligomer as an active form under both nutrient-rich and nutrient-depleted conditions via its amino- and carboxyl-terminal domains independently. Furthermore, we found that a mutant in which the PAS-A domain was deleted was still able to induce sporulation at a wild-type level irrespective of nutrient availability, suggesting that PAS-BC domains are sufficient to maintain the kinase activity. Based on these results, we propose that the primary role of the amino-terminal sensor domain is to form a stable complex as a functional kinase, but possibly not for the binding of an unidentified sporulation signal(s).
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