ArticleMolecular microbiology2012
Elucidation of the multiple roles of CheD in Bacillus subtilis chemotaxis.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Review
- CheD is a Key Protein Involved in Regulating the Chemotaxis and Pathogenic Life Cycle of Agrobacterium fabrum.Current microbiology · 2025Article
- Pseudomonas cultivated from Andropogon gerardii rhizosphere show functional potential for promoting plant host growth and drought resilience.BMC genomics · 2022Article
- Deciphering the Che2 chemosensory pathway and the roles of individual Che2 proteins from Pseudomonas aeruginosa.Molecular microbiology · 2021Article
- Cellular Stoichiometry of Chemotaxis Proteins inJournal of bacteriology · 2020Article
- The Mechanism of Bidirectional pH Taxis in Bacillus subtilis.Journal of bacteriology · 2020Article
- Logarithmic sensing inNPJ systems biology and applications · 2017Article
- Borrelia burgdorferi CheD Promotes Various Functions in Chemotaxis and the Pathogenic Life Cycle of the Spirochete.Infection and immunity · 2016Article
- Internal sense of direction: sensing and signaling from cytoplasmic chemoreceptors.Microbiology and molecular biology reviews : MMBR · 2014Review
- Structure and activity of the flagellar rotor protein FliY: a member of the CheC phosphatase family.The Journal of biological chemistry · 2013Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Chemotaxis by Bacillus subtilis requires the CheD protein for proper function. In a cheD mutant when McpB was the sole chemoreceptor in B. subtilis, chemotaxis to asparagine was quite good. When McpC was the sole chemoreceptor in a cheD mutant, chemotaxis to proline was very poor. The reason for the difference between the chemoreceptors is because CheD deamidates Q609 in McpC and does not deamidate McpB. When mcpC-Q609E is expressed as the sole chemoreceptor in a cheD background, chemotaxis is almost fully restored. Concomitantly, in vitro McpC activates the CheA kinase poorly, whereas McpC-Q609E activates it much more. Moreover, CheD, which activates chemoreceptors, binds better to McpC-Q609E compared with unmodified McpC. Using hydroxyl radical susceptibility in the presence or absence of CheD, the most likely sites of CheD binding were the modification sites where CheD, CheB and CheR carry out their catalytic activities. Thus, CheD appears to have two separate roles in B. subtilis chemotaxis - to bind to chemoreceptors to activate them as part of the CheC/CheD/CheYp adaptation system and to deamidate selected residues to activate the chemoreceptors and enable them to mediate amino acid chemotaxis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.