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PMID:23056386
| Citation |
Little, R, Slavny, P and Dixon, R (2012) Influence of PAS domain flanking regions on oligomerisation and redox signalling by NifL. PLoS ONE 7:e46651 |
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| 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. |
| Links |
PubMed PMC3466315 Online version:10.1371/journal.pone.0046651 |
| Keywords |
Amino Acid Sequence; Azotobacter vinelandii/chemistry; Azotobacter vinelandii/genetics; Azotobacter vinelandii/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Blotting, Western; Chromatography, Gel; Gene Expression Regulation, Bacterial/genetics; Gene Expression Regulation, Bacterial/physiology; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Multimerization/genetics; Protein Multimerization/physiology; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Signal Transduction/genetics; Signal Transduction/physiology |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0030528: transcription regulator activity |
ECO:0000315: |
F |
Figure. 3 N-terminal truncations affect the ability of NifL to regulate transcriptional activation by NifA |
complete | ||||
See also
References
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