Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.12540/51
DC Field | Value | Language |
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dc.contributor.author | Zarban, Randa | en_US |
dc.contributor.author | Vogler, Malvina | en_US |
dc.contributor.author | Wong, Aloysius | en_US |
dc.contributor.author | Eppinger, Joerg | en_US |
dc.contributor.author | Al-Babili, Salim | en_US |
dc.contributor.author | Gehring, Chris | en_US |
dc.date.accessioned | 2020-06-19T02:12:56Z | - |
dc.date.available | 2020-06-19T02:12:56Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Zarban, R., Vogler, M., Wong, A., Eppinger, J., Al-Babili, S., & Gehring, C. (2019). Discovery of a nitric oxide-responsive protein in Arabidopsis thaliana. Molecules, 24(15), 2691. | en_US |
dc.identifier.uri | https://hdl.handle.net/20.500.12540/51 | - |
dc.description.abstract | In plants, much like in animals, nitric oxide (NO) has been established as an important gaseous signaling molecule. However, contrary to animal systems, NO-sensitive or NO-responsive proteins that bind NO in the form of a sensor or participating in redox reactions have remained elusive. Here, we applied a search term constructed based on conserved and functionally annotated amino acids at the centers of Heme Nitric Oxide/Oxygen (H-NOX) domains in annotated and experimentally-tested gas-binding proteins from lower and higher eukaryotes, in order to identify candidate NO-binding proteins in Arabidopsis thaliana. The selection of candidate NO-binding proteins identified from the motif search was supported by structural modeling. This approach identified AtLRB3 (At4g01160), a member of the Light Response Bric-a-Brac/Tramtrack/Broad Complex (BTB) family, as a candidate NO-binding protein. AtLRB3 was heterologously expressed and purified, and then tested for NO-response. Spectroscopic data confirmed that AtLRB3 contains a histidine-ligated heme cofactor and importantly, the addition of NO to AtLRB3 yielded absorption characteristics reminiscent of canonical H-NOX proteins. Furthermore, substitution of the heme iron-coordinating histidine at the H-NOX center with a leucine strongly impaired the NO-response. Our finding therefore established AtLRB3 as a NO-interacting protein and future characterizations will focus on resolving the nature of this response. | en_US |
dc.format.extent | 17 pages | en_US |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartof | Molecules | en_US |
dc.rights.uri | https://creativecommons.org/licenses/by-nc/4.0/ | - |
dc.subject.lcsh | Arabidopsis Thaliana | en_US |
dc.subject.lcsh | Nitric Oxide | en_US |
dc.title | Discovery of a nitric oxide-responsive protein in Arabidopsis thaliana | en_US |
dc.type | Article | en_US |
dc.rights.license | Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) | en_US |
dc.identifier.doi | 10.3390/molecules24152691 | - |
dc.subject.keywords | Heme Nitric Oxide | en_US |
dc.subject.keywords | NO-sensitive Protein | en_US |
dc.subject.keywords | Tramtrack | en_US |
dc.subject.keywords | Broad Complex | en_US |
dc.subject.keywords | Oxygen (H-NOX) Domain | en_US |
dc.subject.keywords | Bric-a-Brac | en_US |
Appears in Collections: | Scholarly Publications |
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File | Description | Size | Format | |
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wku_schlrs_publcn_000026.pdf | 2.45 MB | Adobe PDF | View/Open |
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