ArticlePloS one2012
Influence of PAS domain flanking regions on oligomerisation and redox signalling by NifL.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Sensing the Reducing Power to Determine the Cell Fate: Flavin Redox-Switches in Signal Transduction.Current microbiology · 2025Review
- A Two-Protein Chemoreceptor Complex Regulates Oxygen Thresholds in Bacterial Magneto-Aerotaxis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structural insights into redox signal transduction mechanisms in the control of nitrogen fixation by the NifLA system.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular Mechanism and Agricultural Application of the NifA-NifL System for Nitrogen Fixation.International journal of molecular sciences · 2023Review
- Subtle sequence differences between two interacting σThe FEBS journal · 2022Article
- Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019Review
- Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Coiled-coil dimerization of the LOV2 domain of the blue-light photoreceptor phototropin 1 from Arabidopsis thaliana.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Charting the signal trajectory in a light-oxygen-voltage photoreceptor by random mutagenesis and covariance analysis.The Journal of biological chemistry · 2013Article
- Characterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmission.BMC microbiology · 2013Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Per-ARNT-Sim (PAS) domains constitute a typically dimeric, conserved α/β tertiary fold of approximately 110 amino acids that perform signalling roles in diverse proteins from all kingdoms of life. The amino terminal PAS1 domain of NifL from Azotobacter vinelandii accommodates a redox-active FAD group; elevation of cytosolic oxygen concentrations result in FAD oxidation and a concomitant conformational re-arrangement that is relayed via a short downstream linker to a second PAS domain, PAS2. At PAS2, the signal is amplified and passed on to effector domains generating the 'on' (inhibitory) state of the protein. Although the crystal structure of oxidised PAS1 reveals regions that contribute to the dimerisation interface, 21 amino acids at the extreme N-terminus of NifL, are unresolved. Furthermore, the structure and function of the linker between the two PAS domains has not been determined. In this study we have investigated the importance to signalling of residues extending beyond the core PAS fold. Our results implicate the N-terminus of PAS1 and the helical linker connecting the two PAS domains in redox signal transduction and demonstrate a role for these flanking regions in controlling the oligomerisation state of PAS1 in solution.
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