N- and C-Terminal Flanking Regions Modulate Light-Induced Signal Transduction in the LOV2 Domain of the Blue Light Sensor Phototropin 1 from Avena sativa ,
Abstract
Light sensing by photoreceptors controls phototropism, chloroplast movement, stomatal opening, and leaf expansion in plants. Understanding the molecular mechanism by which these processes are regulated requires a quantitative description of photoreceptor dynamics. We focus on a light-driven signal transduction mechanism in the LOV2 domain (LOV, light, oxygen, voltage) of the blue light photoreceptor phototropin 1 from Avena sativa (oat). High-resolution crystal structures of the dark and light states of an oat LOV2 construct including residues Leu404 through Leu546 (LOV2 (404-546)) have been determined at 105 and 293 K. In all four structures, LOV2 (404-546) exhibits the typical Per-ARNT-Sim (PAS) fold, flanked by an additional conserved N-terminal turn-helix-turn motif and a C-terminal flanking region containing an amphipathic Jalpha helix. These regions dock on the LOV2 core domain and bury several hydrophobic residues of the central beta-sheet of the core domain that would otherwise be exposed to solvent. Light structures of LOV2 (404-546) reveal that formation of the covalent bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangement of the hydrogen-bonding network in the FMN binding pocket. These rearrangements are associated with disruption of the Asn414-Asp515 hydrogen bond on the surface of the protein and displacement of the N- and C-terminal flanking regions of LOV2 (404-546), both of which constitute a structural signal.
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Blue light induces conformational changes in LOV2 to enhance STK phosphorylation.
“Through high-resolution crystal structure analysis and spectroscopic measurements, blue light was found to induce conformational changes in the LOV2 to enhance STK phosphorylation (Iwata et al., 2003; Halavaty and Moffat, 2007; Liscum et al., 2014).”
From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Halavaty and Moffat, 2007
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- Authors
- Halavaty, A. S., & Moffat, K.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Moffat, Keith
- ORCID
- Moffat, Keith
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-11-15
- Volume
- 46
- Issue
- 49
- Pages
- 14001-14009
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2096165020
- Cited by
- 317
- References
- 50
- Citations by year
- 2026: 14 · 2025: 11 · 2024: 16 · 2023: 28 · 2022: 12 · 2021: 22 · 2020: 27 · 2019: 19 · 2018: 9 · 2017: 10 · 2016: 13 · 2015: 18 · 2014: 19 · 2013: 20 · 2012: 22
- FWCI
- 15.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM 036452)
- National Center for Research Resources (RR07 707)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- phototropin 1, LOV2 domain, blue-light photoreceptor, Avena sativa, flavin mononucleotide, hydrogen bond network, protein crystal structure, light-induced conformational change, phototropism
- MeSH terms
- Amino Acid Sequence, Darkness, Flavoproteins, Light, Models, Molecular, Molecular Sequence Data, Signal Transduction, Sequence Alignment, Protein Structure, Tertiary, Crystallography, X-Ray, Avena, Photosynthetic Reaction Center Complex Proteins, Cryptochromes
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