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Papiz, MZ, Bellini, D, Evans, K, Grossmann, G and Fordham-Skelton, T (2019) Light-induced complex formation of bacteriophytochrome RpBphP1 and gene repressor RpPpsR2 probed by SAXS. The FEBS Journal. ISSN 1742-464X
Full text not available from this repository. Please see publisher or open access link below:Abstract
Bacteriophytochrome proteins (BphPs) are molecular light switches that enable organisms to adapt to changing light conditions through the control of gene expression. Canonical type 1 BphPs have histidine kinase output domains, but type 3 RpBphP1, in the bacterium Rhodopseudomonas palustris (Rps. palustris), has a C terminal PAS9 domain and a two‐helix output sensor (HOS) domain. Type 1 BphPs form head‐to‐head parallel dimers; however, the crystal structure of RpBphP1ΔHOS, which does not contain the HOS domain, revealed pseudo anti‐parallel dimers. HOS domains are homologs of Dhp dimerization domains in type 1 BphPs. We show, by applying the small angle X‐ray scattering (SAXS) technique on full‐length RpBphP1, that HOS domains fulfill a similar role in the formation of parallel dimers. On illumination with far‐red light, RpBphP1 forms a complex with gene repressor RpPpsR2 through light‐induced structural changes in its HOS domains. An RpBphP1:RpPpsR2 complex is formed in the molecular ratio of 2 : 1 such that one RpBphP1 dimer binds one RpPpsR2 monomer. Molecular dimers have been modeled with Pfr and Pr SAXS data, suggesting that, in the Pfr state, stable dimeric four α‐helix bundles are formed between HOS domains, rendering RpBphP1functionally inert. On illumination with light of 760 nm wavelength, four α‐helix bundles formed by HOS dimers are disrupted, rendering helices available for binding with RpPpsR2.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | 0601 Biochemistry and Cell Biology, 1101 Medical Biochemistry and Metabolomics, 0304 Medicinal and Biomolecular Chemistry |
| Subjects: | Q Science > QR Microbiology R Medicine > RM Therapeutics. Pharmacology |
| Divisions: | Pharmacy & Biomolecular Sciences |
| Publisher: | Wiley |
| Related URLs: | |
| Date Deposited: | 07 Oct 2019 10:51 |
| Last Modified: | 03 Sep 2021 22:55 |
| DOI or ID number: | 10.1111/febs.14973 |
| URI: | https://researchonline.ljmu.ac.uk/id/eprint/11478 |
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