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Open AccessArticle

Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana

1
Division of Biological and Environmental Science and Engineering, King Abdullah University of Science and Technology, 23955-6900 Thuwal, Saudi Arabia
2
Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85748 Garching, Germany
3
College of Science and Technology, Wenzhou-Kean University, 88 Daxue Road, Ouhai, Wenzhou 325060, Zhejiang, China
4
Department of Chemistry, Biology & Biotechnology, University of Perugia, Borgo XX giugno, 74, 06121 Perugia, Italy
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2019, 24(15), 2691; https://doi.org/10.3390/molecules24152691
Received: 16 June 2019 / Revised: 20 July 2019 / Accepted: 22 July 2019 / Published: 24 July 2019
(This article belongs to the Section Chemical Biology)
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. View Full-Text
Keywords: Arabidopsis thaliana; nitric oxide; Heme Nitric Oxide/Oxygen (H-NOX) domain; Bric-a-Brac/Tramtrack/Broad Complex (BTB); NO-sensitive protein Arabidopsis thaliana; nitric oxide; Heme Nitric Oxide/Oxygen (H-NOX) domain; Bric-a-Brac/Tramtrack/Broad Complex (BTB); NO-sensitive protein
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MDPI and ACS Style

Zarban, R.; Vogler, M.; Wong, A.; Eppinger, J.; Al-Babili, S.; Gehring, C. Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana. Molecules 2019, 24, 2691. https://doi.org/10.3390/molecules24152691

AMA Style

Zarban R, Vogler M, Wong A, Eppinger J, Al-Babili S, Gehring C. Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana. Molecules. 2019; 24(15):2691. https://doi.org/10.3390/molecules24152691

Chicago/Turabian Style

Zarban, Randa; Vogler, Malvina; Wong, Aloysius; Eppinger, Joerg; Al-Babili, Salim; Gehring, Chris. 2019. "Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana" Molecules 24, no. 15: 2691. https://doi.org/10.3390/molecules24152691

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