ArticleThe Journal of biological chemistry2010
Transmembrane signaling in chimeras of the Escherichia coli aspartate and serine chemotaxis receptors and bacterial class III adenylyl cyclases.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- The evolutionary conservation of eukaryotic membrane-bound adenylyl cyclase isoforms.Frontiers in pharmacology · 2022Pooled it
- Lipid regulation of adenylyl cyclase Rv1625c from Mycobacterium tuberculosis by its membrane-domain receptor.The FEBS journal · 2025Article
- Article
- Article
- The YHS-Domain of an Adenylyl Cyclase from Mycobacterium phlei Is a Probable Copper-Sensor Module.PloS one · 2015Article
- Engineering adenylate cyclases regulated by near-infrared window light.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- HAMP domain signal relay mechanism in a sensory rhodopsin-transducer complex.The Journal of biological chemistry · 2012Article
- The S-helix determines the signal in a Tsr receptor/adenylyl cyclase reporter.The Journal of biological chemistry · 2012Article
- Crystal structure and regulation mechanisms of the CyaB adenylyl cyclase from the human pathogen Pseudomonas aeruginosa.Journal of molecular biology · 2012Article
- HAMP domain-mediated signal transduction probed with a mycobacterial adenylyl cyclase as a reporter.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli chemoreceptors for serine (Tsr) and aspartate (Tar) and several bacterial class III adenylyl cyclases (ACs) share a common molecular architecture; that is, a membrane anchor that is linked via a cytoplasmic HAMP domain to a C-terminal signal output unit. Functionality of both proteins requires homodimerization. The chemotaxis receptors are well characterized, whereas the typical hexahelical membrane anchor (6TM) of class III ACs, suggested to operate as a channel or transporter, has no known function beyond a membrane anchor. We joined the intramolecular networks of Tsr or Tar and two bacterial ACs, Rv3645 from Mycobacterium tuberculosis and CyaG from Arthrospira platensis, across their signal transmission sites, connecting the chemotaxis receptors via different HAMP domains to the catalytic AC domains. AC activity in the chimeras was inhibited by micromolar concentrations of l-serine or l-aspartate in vitro and in vivo. Single point mutations known to abolish ligand binding in Tar (R69E or T154I) or Tsr (R69E or T156K) abrogated AC regulation. Co-expression of mutant pairs, which functionally complement each other, restored regulation in vitro and in vivo. Taken together, these studies demonstrate chemotaxis receptor-mediated regulation of chimeric bacterial ACs and connect chemical sensing and AC regulation.
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