ArticleThe Journal of biological chemistry2012
The S-helix determines the signal in a Tsr receptor/adenylyl cyclase reporter.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.
- The evolutionary conservation of eukaryotic membrane-bound adenylyl cyclase isoforms.Frontiers in pharmacology · 2022Pooled it
- Protein design-scapes generated by microfluidic DNA assembly elucidate domain coupling in the bacterial histidine kinase CpxA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- CaFrontiers in molecular neuroscience · 2018Article
- Molecular Mechanisms of Two-Component Signal Transduction.Journal of molecular biology · 2016Review
- Article
- Signal transduction in histidine kinases: insights from new structures.Structure (London, England : 1993) · 2015Review
- Engineering adenylate cyclases regulated by near-infrared window light.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Engineering of a red-light-activated human cAMP/cGMP-specific phosphodiesterase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Nitric oxide-induced conformational changes in soluble guanylate cyclase.Structure (London, England : 1993) · 2014Article
- Charting the signal trajectory in a light-oxygen-voltage photoreceptor by random mutagenesis and covariance analysis.The Journal of biological chemistry · 2013Article
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
A signaling or S-helix has been identified as a conserved, up to 50-residue-long segment in diverse sensory proteins. It is present in all major bacterial lineages and in euryarchea and eukaryotes. A bioinformatic analysis shows that it connects upstream receiver and downstream output domains, e.g. in histidine kinases and bacterial adenylyl cyclases. The S-helix is modeled as a two-helical parallel coiled coil. It is predicted to prevent constitutive activation of the downstream signaling domains in the absence of ligand-binding. We identified an S-helix of about 25 residues in the adenylyl cyclase CyaG from Arthrospira maxima. Deletion of the 25 residue segment connecting the HAMP and catalytic domains in a chimera with the Escherichia coli Tsr receptor changed the response to serine from inhibition to stimulation. Further examination showed that a deletion of one to three heptads plus a presumed stutter, i.e. 1, 2, or 3 × 7 + 4 amino acids, is required and sufficient for signal reversion. It was not necessary that the deletions be continuous, as removal of separated heptads and presumed stutters also resulted in signal reversion. Furthermore, insertion of the above segments between the HAMP and cyclase catalytic domains similarly resulted in signal reversion. This indicates that the S-helix is an independent, segmented module capable to reverse the receptor signal. Because the S-helix is present in all kingdoms of life, e.g. in human retinal guanylyl cyclase, our findings may be significant for many sensory systems.
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