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1

LeCuyer, Brian E., Alison K. Criss, and H. Steven Seifert. "Genetic Characterization of the Nucleotide Excision Repair System of Neisseria gonorrhoeae." Journal of Bacteriology 192, no. 3 (November 20, 2009): 665–73. http://dx.doi.org/10.1128/jb.01018-09.

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ABSTRACT Nucleotide excision repair (NER) is universally used to recognize and remove many types of DNA damage. In eubacteria, the NER system typically consists of UvrA, UvrB, UvrC, the UvrD helicase, DNA polymerase I, and ligase. In addition, when DNA damage blocks transcription, transcription-repair coupling factor (TRCF), the product of the mfd gene, recruits the Uvr complex to repair the damage. Previous work using selected mutants and assays have indicated that pathogenic Neisseria spp. carry a functional NER system. In order to comprehensively examine the role of NER in Neisseria gonorrhoeae DNA recombination and repair processes, the predicted NER genes (uvrA, uvrB, uvrC, uvrD, and mfd) were each disrupted by a transposon insertion, and the uvrB and uvrD mutants were complemented with a copy of each gene in an ectopic locus. Each uvr mutant strain was highly sensitive to UV irradiation and also showed sensitivity to hydrogen peroxide killing, confirming that all of the NER genes in N. gonorrhoeae are functional. The effect of RecA expression on UV survival was minor in uvr mutants but much larger in the mfd mutant. All of the NER mutants demonstrated wild-type levels of pilin antigenic variation and DNA transformation. However, the uvrD mutant exhibited higher frequencies of PilC-mediated pilus phase variation and spontaneous mutation, a finding consistent with a role for UvrD in mismatch repair. We conclude that NER functions are conserved in N. gonorrhoeae and are important for the DNA repair capabilities of this strict human pathogen.
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2

Moolenaar, Geri F., Celine Moorman, and Nora Goosen. "Role of the Escherichia coli Nucleotide Excision Repair Proteins in DNA Replication." Journal of Bacteriology 182, no. 20 (October 15, 2000): 5706–14. http://dx.doi.org/10.1128/jb.182.20.5706-5714.2000.

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ABSTRACT DNA polymerase I (PolI) functions both in nucleotide excision repair (NER) and in the processing of Okazaki fragments that are generated on the lagging strand during DNA replication.Escherichia coli cells completely lacking the PolI enzyme are viable as long as they are grown on minimal medium. Here we show that viability is fully dependent on the presence of functional UvrA, UvrB, and UvrD (helicase II) proteins but does not require UvrC. In contrast, ΔpolA cells grow even better when theuvrC gene has been deleted. Apparently UvrA, UvrB, and UvrD are needed in a replication backup system that replaces the PolI function, and UvrC interferes with this alternative replication pathway. With specific mutants of UvrC we could show that the inhibitory effect of this protein is related to its catalytic activity that on damaged DNA is responsible for the 3′ incision reaction. Specific mutants of UvrA and UvrB were also studied for their capacity to support the PolI-independent replication. Deletion of the UvrC-binding domain of UvrB resulted in a phenotype similar to that caused by deletion of the uvrC gene, showing that the inhibitory incision activity of UvrC is mediated via binding to UvrB. A mutation in the N-terminal zinc finger domain of UvrA does not affect NER in vivo or in vitro. The same mutation, however, does give inviability in combination with the ΔpolA mutation. Apparently the N-terminal zinc-binding domain of UvrA has specifically evolved for a function outside DNA repair. A model for the function of the UvrA, UvrB, and UvrD proteins in the alternative replication pathway is discussed.
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3

Yin, Ruohe, Mariya Y. Skvortsova, Sylvain Loubéry, and Roman Ulm. "COP1 is required for UV-B–induced nuclear accumulation of the UVR8 photoreceptor." Proceedings of the National Academy of Sciences 113, no. 30 (July 12, 2016): E4415—E4422. http://dx.doi.org/10.1073/pnas.1607074113.

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The UV-B photoreceptor UV RESISTANCE LOCUS 8 (UVR8) promotes UV-B acclimation and tolerance in Arabidopsis thaliana. UVR8 localizes to both cytosol and nucleus, but its main activity is assumed to be nuclear. UV-B photoreception stimulates nuclear accumulation of UVR8 in a presently unknown manner. Here, we show that CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1) is required for UV-B–induced nuclear accumulation of UVR8, but bypassing the COP1 requirement for UVR8 nuclear accumulation did not rescue the cop1 mutant UV-B phenotype. Using a glucocorticoid receptor (GR)-based fusion protein system to conditionally localize GR-UVR8 to the nucleus, we have demonstrated that both photoactivation and nuclear localization of UVR8 are required for UV-B–induced photomorphogenic responses. In contrast, there was no UV-B response when UV-B–activated UVR8 was artificially retained in the cytosol. In agreement with a predominantly nuclear activity, constitutively active UVR8W285A accumulated in the nucleus also in the absence of UV-B. Furthermore, GR-COP1 expression lines suggested that UV-B–activated UVR8 can be coimported into the nucleus by COP1. Our data strongly support localization of UVR8 signaling in the nucleus and a dual role for COP1 in the regulation of UV-B–induced UVR8 nuclear accumulation and in UVR8-mediated UV-B signaling.
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4

Rai, Neha, Susanne Neugart, Yan Yan, Fang Wang, Sari M. Siipola, Anders V. Lindfors, Jana Barbro Winkler, et al. "How do cryptochromes and UVR8 interact in natural and simulated sunlight?" Journal of Experimental Botany 70, no. 18 (May 17, 2019): 4975–90. http://dx.doi.org/10.1093/jxb/erz236.

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AbstractCryptochromes (CRYs) and UV RESISTANCE LOCUS 8 (UVR8) photoreceptors perceive UV-A/blue (315–500 nm) and UV-B (280–315 nm) radiation in plants, respectively. While the roles of CRYs and UVR8 have been studied in separate controlled-environment experiments, little is known about the interaction between these photoreceptors. Here, Arabidopsis wild-type Ler, CRYs and UVR8 photoreceptor mutants (uvr8-2, cry1cry2 and cry1cry2uvr8-2), and a flavonoid biosynthesis-defective mutant (tt4) were grown in a sun simulator. Plants were exposed to filtered radiation for 17 d or for 6 h, to study the effects of blue, UV-A, and UV-B radiation. Both CRYs and UVR8 independently enabled growth and survival of plants under solar levels of UV, while their joint absence was lethal under UV-B. CRYs mediated gene expression under blue light. UVR8 mediated gene expression under UV-B radiation, and in the absence of CRYs, also under UV-A. This negative regulation of UVR8-mediated gene expression by CRYs was also observed for UV-B. The accumulation of flavonoids was also consistent with this interaction between CRYs and UVR8. In conclusion, we provide evidence for an antagonistic interaction between CRYs and UVR8 and a role of UVR8 in UV-A perception.
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5

Podolec, Roman, Kelvin Lau, Timothée B. Wagnon, Michael Hothorn, and Roman Ulm. "A constitutively monomeric UVR8 photoreceptor confers enhanced UV-B photomorphogenesis." Proceedings of the National Academy of Sciences 118, no. 6 (February 4, 2021): e2017284118. http://dx.doi.org/10.1073/pnas.2017284118.

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The plant ultraviolet-B (UV-B) photoreceptor UVR8 plays an important role in UV-B acclimation and survival. UV-B absorption by homodimeric UVR8 induces its monomerization and interaction with the E3 ubiquitin ligase COP1, leading ultimately to gene expression changes. UVR8 is inactivated through redimerization, facilitated by RUP1 and RUP2. Here, we describe a semidominant, hyperactive allele, namely uvr8-17D, that harbors a glycine-101 to serine mutation. UVR8G101S overexpression led to weak constitutive photomorphogenesis and extreme UV-B responsiveness. UVR8G101S was observed to be predominantly monomeric in vivo and, once activated by UV-B, was not efficiently inactivated. Analysis of a UVR8 crystal structure containing the G101S mutation revealed the distortion of a loop region normally involved in stabilization of the UVR8 homodimer. Plants expressing a UVR8 variant combining G101S with the previously described W285A mutation exhibited robust constitutive photomorphogenesis. This work provides further insight into UVR8 activation and inactivation mechanisms and describes a genetic tool for the manipulation of photomorphogenic responses.
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6

Podolec, Roman, Emilie Demarsy, and Roman Ulm. "Perception and Signaling of Ultraviolet-B Radiation in Plants." Annual Review of Plant Biology 72, no. 1 (June 17, 2021): 793–822. http://dx.doi.org/10.1146/annurev-arplant-050718-095946.

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Ultraviolet-B (UV-B) radiation is an intrinsic fraction of sunlight that plants perceive through the UVR8 photoreceptor. UVR8 is a homodimer in its ground state that monomerizes upon UV-B photon absorption via distinct tryptophan residues. Monomeric UVR8 competitively binds to the substrate binding site of COP1, thus inhibiting its E3 ubiquitin ligase activity against target proteins, which include transcriptional regulators such as HY5. The UVR8–COP1 interaction also leads to the destabilization of PIF bHLH factor family members. Additionally, UVR8 directly interacts with and inhibits the DNA binding of a different set of transcription factors. Each of these UVR8 signaling mechanisms initiates nuclear gene expression changes leading to UV-B-induced photomorphogenesis and acclimation. The two WD40-repeat proteins RUP1 and RUP2 provide negative feedback regulation and inactivate UVR8 by facilitating redimerization. Here, we review the molecular mechanisms of the UVR8 pathway from UV-B perception and signal transduction to gene expression changes and physiological UV-B responses.
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7

Zhang, Zhenhua, Chenjie Xu, Shiyu Zhang, Chen Shi, Hong Cheng, Hongtao Liu, and Bojian Zhong. "Origin and adaptive evolution of UV RESISTANCE LOCUS 8-mediated signaling during plant terrestrialization." Plant Physiology 188, no. 1 (October 18, 2021): 332–46. http://dx.doi.org/10.1093/plphys/kiab486.

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Abstract UV RESISTANCE LOCUS 8 (UVR8) mediates photomorphogenic responses and acclimation to UV-B radiation by regulating the transcription of a series of transcription factors (TFs). However, the origin and evolution of UVR8-mediated signaling pathways remain largely unknown. In this study, we investigated the origin and evolution of the major components of the UVR8-mediated signaling pathway (UVR8, REPRESSOR OF UV-B PHOTOMORPHOGENESIS [RUP], BRI1-EMS-SUPPRESSOR1 [BES1], BES1-INTERACTING MYC-LIKE 1 (BIM1), WRKY DNA-BINDING PROTEIN 36 (WRKY36), MYB DOMAIN PROTEIN 73/77/13 [MYB73/MYB77/MYB13], and PHYTOCHROME INTERACTING FACTOR 4/5 [PIF4 and PIF5]) using comparative genomics and phylogenetic approaches. We showed that the central regulator UVR8 presented a conservative evolutionary route during plant evolution, and the evolutionary history of downstream negative regulators and TFs was different from that of green plant phylogeny. The canonical UVR8-CONSTITUTIVELY PHOTOMORPHOGENIC 1(COP1)/SUPPRESSOR OF PHYA-105 (SPA)-ELONGATED HYPOCOTYL 5 (HY5)-RUP signaling pathway originated in chlorophytes and conferred green algae the additional ability to cope with UV-B radiation. Moreover, the emergence of multiple UVR8-mediated signaling pathways in charophytes laid the foundations for the cross-talk between UV-B signals and endogenous hormone responses. Importantly, we observed signatures that reflect plant adaptations to high UV-B irradiance in subaerial/terrestrial environments, including positive selection in UVR8 and RUPs and increased copy number of some vital TFs. These results revealed that green plants not only experienced adaptive modifications in the canonical UVR8-COP1/SPA-HY5-RUP signaling pathway, but also diversified their UV-B signal transduction mechanisms through increasing cross-talk with other pathways, such as those associated with brassinosteroids and auxin. This study greatly expands our understanding of molecular evolution and adaptive mechanisms underlying plant UV-B acclimation.
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8

Díaz-Ramos, L. Aranzazú, Andrew O'Hara, Selvaraju Kanagarajan, Daniel Farkas, Åke Strid, and Gareth I. Jenkins. "Difference in the action spectra for UVR8 monomerisation and HY5 transcript accumulation in Arabidopsis." Photochemical & Photobiological Sciences 17, no. 8 (2018): 1108–17. http://dx.doi.org/10.1039/c8pp00138c.

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9

Heilmann, Monika, John M. Christie, John T. M. Kennis, Gareth I. Jenkins, and Tilo Mathes. "Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy." Photochemical & Photobiological Sciences 14, no. 2 (2015): 252–57. http://dx.doi.org/10.1039/c4pp00246f.

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The plant photoreceptor UVR8 uses tryptophan side chains to absorb UV-B radiation to induce photoprotective responses via a so far unknown molecular signaling mechanism. We investigated structural transformations and quantum efficiency of UVR8 photoactivation by vibrational and fluorescence spectroscopy.
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10

Camacho, Inês S., Alina Theisen, Linus O. Johannissen, L. Aranzazú Díaz-Ramos, John M. Christie, Gareth I. Jenkins, Bruno Bellina, Perdita Barran, and Alex R. Jones. "Native mass spectrometry reveals the conformational diversity of the UVR8 photoreceptor." Proceedings of the National Academy of Sciences 116, no. 4 (January 4, 2019): 1116–25. http://dx.doi.org/10.1073/pnas.1813254116.

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UVR8 is a plant photoreceptor protein that regulates photomorphogenic and protective responses to UV light. The inactive, homodimeric state absorbs UV-B light, resulting in dissociation into monomers, which are considered to be the active state and comprise a β-propeller core domain and intrinsically disordered N- and C-terminal tails. The C terminus is required for functional binding to signaling partner COP1. To date, however, structural studies have only been conducted with the core domain where the terminal tails have been truncated. Here, we report structural investigations of full-length UVR8 using native ion mobility mass spectrometry adapted for photoactivation. We show that, while truncated UVR8 photoconverts from a single conformation of dimers to a single monomer conformation, the full-length protein exists in numerous conformational families. The full-length dimer adopts both a compact state and an extended state where the C terminus is primed for activation. In the monomer the extended C terminus destabilizes the core domain to produce highly extended yet stable conformations, which we propose are the fully active states that bind COP1. Our results reveal the conformational diversity of full-length UVR8. We also demonstrate the potential power of native mass spectrometry to probe functionally important structural dynamics of photoreceptor proteins throughout nature.
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11

Chen, Daniel, Emily S. Gibson, and Matthew J. Kennedy. "A light-triggered protein secretion system." Journal of Cell Biology 201, no. 4 (May 13, 2013): 631–40. http://dx.doi.org/10.1083/jcb.201210119.

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Optical control of protein interactions has emerged as a powerful experimental paradigm for manipulating and studying various cellular processes. Tools are now available for controlling a number of cellular functions, but some fundamental processes, such as protein secretion, have been difficult to engineer using current optical tools. Here we use UVR8, a plant photoreceptor protein that forms photolabile homodimers, to engineer the first light-triggered protein secretion system. UVR8 fusion proteins were conditionally sequestered in the endoplasmic reticulum, and a brief pulse of light triggered robust forward trafficking through the secretory pathway to the plasma membrane. UVR8 was not responsive to excitation light used to image cyan, green, or red fluorescent protein variants, allowing multicolor visualization of cellular markers and secreted protein cargo as it traverses the cellular secretory pathway. We implemented this novel tool in neurons to demonstrate restricted, local trafficking of secretory cargo near dendritic branch points.
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12

Wu, Qi, Bolong Huang, T. A. Niehaus, Xiaojing Yang, Jun Fan, and Rui-Qin Zhang. "The role of tryptophans in the UV-B absorption of a UVR8 photoreceptor – a computational study." Physical Chemistry Chemical Physics 17, no. 16 (2015): 10786–94. http://dx.doi.org/10.1039/c4cp06073c.

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13

Jawad, Aarrouf, Hdech Douae Ben, Diot Alice, Bornard Isabelle, Félicie Lauri, and Urban Laurent. "Flashes of UV-C light are perceived by UVR8, the photoreceptor of UV-B light." Journal of Plant Science and Phytopathology 6, no. 2 (November 10, 2022): 151–53. http://dx.doi.org/10.29328/journal.jpsp.1001089.

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Light is an important regulator of plant morphogenesis and plant-pathogen interactions via specific photoreceptors and signaling pathways. Besides visible light, other electromagnetic radiations may play roles, notably ultraviolet (UV) light. The UV part of the electromagnetic spectrum includes UV-A (315 nm - 400 nm), UV-B (280 nm - 315 nm) and UV-C radiations (200 nm - 280 nm). UV-B and UV-C have been reported to increase plant resistance to plant pathogens after the UV perception and signaling stages. The perception of UV-B radiation is achieved by the dimer protein UVR8 (UV RESISTANCE LOCUS 8). Even though the action spectrum of this photoreceptor overlaps in the UV-C domain, it has never been formally demonstrated that UVR8 could also act as a photoreceptor of UV-C light. We provide here original observations showing that UVR8 can indeed perceive UV-C light provided that the latter is in the form of flashes (1s) and not continuous illuminations (the 60s). Our observations also show that the response of UVR8 to flashes of UV-C light is dose-dependent. They could explain why flashes of UV-C light are more effective for stimulating plant defenses than continuous illuminations for the same amount of energy delivered to plants (J/m2). Eventually, our observations support ongoing trials that aim at using UV-C light as an environmental-friendly plant resistance inducer in field conditions.
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14

Rai, Neha, Luis Orlando Morales, and Pedro José Aphalo. "Perception of solar UV radiation by plants: photoreceptors and mechanisms." Plant Physiology 186, no. 3 (April 7, 2021): 1382–96. http://dx.doi.org/10.1093/plphys/kiab162.

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Abstract About 95% of the ultraviolet (UV) photons reaching the Earth’s surface are UV-A (315–400 nm) photons. Plant responses to UV-A radiation have been less frequently studied than those to UV-B (280–315 nm) radiation. Most previous studies on UV-A radiation have used an unrealistic balance between UV-A, UV-B, and photosynthetically active radiation (PAR). Consequently, results from these studies are difficult to interpret from an ecological perspective, leaving an important gap in our understanding of the perception of solar UV radiation by plants. Previously, it was assumed UV-A/blue photoreceptors, cryptochromes and phototropins mediated photomorphogenic responses to UV-A radiation and “UV-B photoreceptor” UV RESISTANCE LOCUS 8 (UVR8) to UV-B radiation. However, our understanding of how UV-A radiation is perceived by plants has recently improved. Experiments using a realistic balance between UV-B, UV-A, and PAR have demonstrated that UVR8 can play a major role in the perception of both UV-B and short-wavelength UV-A (UV-Asw, 315 to ∼350 nm) radiation. These experiments also showed that UVR8 and cryptochromes jointly regulate gene expression through interactions that alter the relative sensitivity to UV-B, UV-A, and blue wavelengths. Negative feedback loops on the action of these photoreceptors can arise from gene expression, signaling crosstalk, and absorption of UV photons by phenolic metabolites. These interactions explain why exposure to blue light modulates photomorphogenic responses to UV-B and UV-Asw radiation. Future studies will need to distinguish between short and long wavelengths of UV-A radiation and to consider UVR8’s role as a UV-B/UV-Asw photoreceptor in sunlight.
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15

Neugart, Susanne, Mark A. Tobler, and Paul W. Barnes. "Different irradiances of UV and PAR in the same ratios alter the flavonoid profiles of Arabidopsis thaliana wild types and UV-signalling pathway mutants." Photochemical & Photobiological Sciences 18, no. 7 (2019): 1685–99. http://dx.doi.org/10.1039/c8pp00496j.

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16

O'Hara, Andrew, Lauren R. Headland, L. Aranzazú Díaz-Ramos, Luis O. Morales, Åke Strid, and Gareth I. Jenkins. "Regulation of Arabidopsis gene expression by low fluence rate UV-B independently of UVR8 and stress signaling." Photochemical & Photobiological Sciences 18, no. 7 (2019): 1675–84. http://dx.doi.org/10.1039/c9pp00151d.

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17

Sun, Kaiwen, and Ziqiang Zhu. "Illuminating the Nucleus: UVR8 Interacts with More." Trends in Plant Science 23, no. 4 (April 2018): 279–81. http://dx.doi.org/10.1016/j.tplants.2018.03.002.

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18

Xu, Yang, and Ziqiang Zhu. "UV-B Response: When UVR8 Meets MYBs." Trends in Plant Science 25, no. 6 (June 2020): 515–17. http://dx.doi.org/10.1016/j.tplants.2020.03.010.

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19

Heijde, M., M. Binkert, R. Yin, F. Ares-Orpel, L. Rizzini, E. Van De Slijke, G. Persiau, et al. "Constitutively active UVR8 photoreceptor variant in Arabidopsis." Proceedings of the National Academy of Sciences 110, no. 50 (November 25, 2013): 20326–31. http://dx.doi.org/10.1073/pnas.1314336110.

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Miyamori, Takaaki, Yusuke Nakasone, Kenichi Hitomi, John M. Christie, Elizabeth D. Getzoff, and Masahide Terazima. "Reaction dynamics of the UV-B photosensor UVR8." Photochemical & Photobiological Sciences 14, no. 5 (2015): 995–1004. http://dx.doi.org/10.1039/c5pp00012b.

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Vanhaelewyn, Lucas, Péter Bernula, Dominique Van Der Straeten, Filip Vandenbussche, and András Viczián. "UVR8-dependent reporters reveal spatial characteristics of signal spreading in plant tissues." Photochemical & Photobiological Sciences 18, no. 5 (2019): 1030–45. http://dx.doi.org/10.1039/c8pp00492g.

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Hall, Barry G. "Genetics of selection-induced mutations: I. uvrA, uvrB, uvrC, and uvrD are selection-induced specific mutator loci." Journal of Molecular Evolution 40, no. 1 (January 1995): 86–93. http://dx.doi.org/10.1007/bf00166599.

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Liao, Xinyang, Ben Zhang, Michael R. Blatt, and Gareth I. Jenkins. "A FRET method for investigating dimer/monomer status and conformation of the UVR8 photoreceptor." Photochemical & Photobiological Sciences 18, no. 2 (2019): 367–74. http://dx.doi.org/10.1039/c8pp00489g.

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Humann, Jodi L., Hope T. Ziemkiewicz, Svetlana N. Yurgel, and Michael L. Kahn. "Regulatory and DNA Repair Genes Contribute to the Desiccation Resistance of Sinorhizobium meliloti Rm1021." Applied and Environmental Microbiology 75, no. 2 (November 21, 2008): 446–53. http://dx.doi.org/10.1128/aem.02207-08.

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ABSTRACT Sinorhizobium meliloti can form a nitrogen-fixing symbiotic relationship with alfalfa after bacteria in the soil infect emerging root hairs of the growing plant. To be successful at this, the bacteria must be able to survive in the soil between periods of active plant growth, including when conditions are dry. The ability of S. meliloti to withstand desiccation has been known for years, but genes that contribute to this phenotype have not been identified. Transposon mutagenesis was used in combination with novel screening techniques to identify four desiccation-sensitive mutants of S. meliloti Rm1021. DNA sequencing of the transposon insertion sites identified three genes with regulatory functions (relA, rpoE2, and hpr) and a DNA repair gene (uvrC). Various phenotypes of the mutants were determined, including their behavior on several indicator media and in symbiosis. All of the mutants formed an effective symbiosis with alfalfa. To test the hypothesis that UvrC-related excision repair was important in desiccation resistance, uvrA, uvrB, and uvrC deletion mutants were also constructed. These strains were sensitive to DNA damage induced by UV light and 4-NQO and were also desiccation sensitive. These data indicate that uvr gene-mediated DNA repair and the regulation of stress-induced pathways are important for desiccation resistance.
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Di Wu, Qi Hu, Zhen Yan, Wen Chen, Chuangye Yan, Xi Huang, Jing Zhang, et al. "Structural basis of ultraviolet-B perception by UVR8." Nature 484, no. 7393 (February 29, 2012): 214–19. http://dx.doi.org/10.1038/nature10931.

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Arongaus, Adriana B., Song Chen, Marie Pireyre, Nina Glöckner, Vinicius C. Galvão, Andreas Albert, J. Barbro Winkler, Christian Fankhauser, Klaus Harter, and Roman Ulm. "ArabidopsisRUP2 represses UVR8-mediated flowering in noninductive photoperiods." Genes & Development 32, no. 19-20 (September 25, 2018): 1332–43. http://dx.doi.org/10.1101/gad.318592.118.

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Jeruzalmi, David. "Inner Workings of the UvrA·UvrB DNA Damage Sensor during Bacterial Nucleotide Excision Repair." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C453. http://dx.doi.org/10.1107/s2053273314095461.

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Efficient elimination of DNA lesions by the nucleotide excision repair (NER) pathway is critical for all organisms. In bacteria, the NER pathway is implemented by the successive action of three proteins, UvrA, UvrB and UvrC via a series of large and dynamic multi-protein complexes. A large number of studies have defined three major stages associated with the early steps of the NER pathway. In stage 1, a large (300-400 kDa) complex of the UvrA and UvrB proteins (AB) scans the genome to identify lesion-containing DNA. This process requires rapid binding and release of DNA; moreover, damage must be specifically recognized, and distinguished from native DNA, despite the fact that the relevant lesions induce widely different DNA structures. Once lesion-containing DNA has been located, it is stably bound by a dimeric form of UvrA within the AB complex (Stage 2). A major reorganization then occurs in which UvrA is lost from the ensemble, and concomitantly, UvrB becomes localized at the site of damage (Stage 3). Following these early stages, additional events lead to excision of the damage on one strand, and repair of the resulting single-stranded gap. Over the past few years, we have determined three structures of UvrA and the UvrA·UvrB complex. Our first structure of isolated UvrA revealed its overall architecture, its DNA binding surface, and the arrangement of its four-nucleotide binding sites. In the structure of the complete UvrA·UvrB damage sensor, a central UvrA dimer is flanked by two UvrB molecules, all linearly arrayed along a DNA path predicted by biochemical studies. DNA is predicted to bind to UvrA in the complex within a narrow and deep groove that is compatible with native duplex DNA only. In contrast, the shape of the corresponding surface in our prior structure of UvrA is wide and shallow, and appears compatible with various types of lesion-deformed DNA. These differences point to conformation switching between the two forms as a component of the genome-scanning phase of damage sensing. We also show that the highly conserved signature domain II of UvrA, which is adjacent to the proximal nucleotide-binding site, mediates a critical nexus of contacts to UvrB and to DNA. Moreover, in the novel UvrA conformer, the disposition of this domain is altered such that association with either UvrB or DNA is precluded. Concomitantly, nucleotide is uniquely absent from the proximal binding site. Thus, the signature domain II is implicated in an ATP-hydrolysis-dependent conformational change that detaches UvrA from both UvrB and DNA after initial damage recognition. The disposition and number of UvrB molecules in the AB complex, both unanticipated, suggest that once UvrA departs, UvrB localizes to the site of damage by helicase-mediated tracking along the DNA. Together these results permit a high-resolution model for the dynamics of early stages in NER.
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Yang, Xiaojing, Sherwin Montano, and Zhong Ren. "How Does Photoreceptor UVR8 Perceive a UV-B Signal?" Photochemistry and Photobiology 91, no. 5 (June 11, 2015): 993–1003. http://dx.doi.org/10.1111/php.12470.

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Tilbrook, Kimberley, Adriana B. Arongaus, Melanie Binkert, Marc Heijde, Ruohe Yin, and Roman Ulm. "The UVR8 UV-B Photoreceptor: Perception, Signaling and Response." Arabidopsis Book 11 (January 2013): e0164. http://dx.doi.org/10.1199/tab.0164.

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Rizzini, L., J. J. Favory, C. Cloix, D. Faggionato, A. O'Hara, E. Kaiserli, R. Baumeister, et al. "Perception of UV-B by the Arabidopsis UVR8 Protein." Science 332, no. 6025 (March 31, 2011): 103–6. http://dx.doi.org/10.1126/science.1200660.

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Liu, Zheyun, Xiankun Li, Frank W. Zhong, Jiang Li, Lijuan Wang, Yigong Shi, and Dongping Zhong. "Quenching Dynamics of Ultraviolet-Light Perception by UVR8 Photoreceptor." Journal of Physical Chemistry Letters 5, no. 1 (December 9, 2013): 69–72. http://dx.doi.org/10.1021/jz402396k.

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32

Hofmann, Nancy R. "The Molecular Mechanism of the UVR8 UV-B Photoreceptor." Plant Cell 24, no. 9 (September 2012): 3485. http://dx.doi.org/10.1105/tpc.112.240910.

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Jenkins, Gareth I. "The UV-B Photoreceptor UVR8: From Structure to Physiology." Plant Cell 26, no. 1 (January 2014): 21–37. http://dx.doi.org/10.1105/tpc.113.119446.

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Jenkins, Gareth I. "Structure and function of the UV-B photoreceptor UVR8." Current Opinion in Structural Biology 29 (December 2014): 52–57. http://dx.doi.org/10.1016/j.sbi.2014.09.004.

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35

Brown, Bobby A., Lauren R. Headland, and Gareth I. Jenkins. "UV-B Action Spectrum for UVR8-MediatedHY5Transcript Accumulation in Arabidopsis." Photochemistry and Photobiology 85, no. 5 (September 2009): 1147–55. http://dx.doi.org/10.1111/j.1751-1097.2009.00579.x.

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Dong, Huaxi, Xiaorui Liu, Chunli Zhang, Huicong Guo, Yang Liu, Huoying Chen, Ruohe Yin, and Li Lin. "Expression of Tomato UVR8 in Arabidopsis reveals conserved photoreceptor function." Plant Science 303 (February 2021): 110766. http://dx.doi.org/10.1016/j.plantsci.2020.110766.

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37

Hayes, Scott, Ashutosh Sharma, Donald P. Fraser, Martine Trevisan, C. Kester Cragg-Barber, Eleni Tavridou, Christian Fankhauser, Gareth I. Jenkins, and Keara A. Franklin. "UV-B Perceived by the UVR8 Photoreceptor Inhibits Plant Thermomorphogenesis." Current Biology 27, no. 1 (January 2017): 120–27. http://dx.doi.org/10.1016/j.cub.2016.11.004.

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Liang, Tong, Yu Yang, and Hongtao Liu. "Signal transduction mediated by the plant UV‐B photoreceptor UVR8." New Phytologist 221, no. 3 (October 13, 2018): 1247–52. http://dx.doi.org/10.1111/nph.15469.

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Li, Xiankun, Zheyun Liu, Haisheng Ren, Mainak Kundu, Lijuan Wang, Jiali Gao, and Dongping Zhong. "Dynamics and mechanism of light harvesting in UV photoreceptor UVR8." Chemical Science 11, no. 46 (2020): 12553–69. http://dx.doi.org/10.1039/d0sc04909c.

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40

Qiu, Xiaoyun, George W. Sundin, Benli Chai, and James M. Tiedje. "Survival of Shewanella oneidensis MR-1 after UV Radiation Exposure." Applied and Environmental Microbiology 70, no. 11 (November 2004): 6435–43. http://dx.doi.org/10.1128/aem.70.11.6435-6443.2004.

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ABSTRACT We systematically investigated the physiological response as well as DNA damage repair and damage tolerance in Shewanella oneidensis MR-1 following UVC, UVB, UVA, and solar light exposure. MR-1 showed the highest UVC sensitivity among Shewanella strains examined, with D37 and D10 values of 5.6 and 16.5% of Escherichia coli K-12 values. Stationary cells did not show an increased UVA resistance compared to exponential-phase cells; instead, they were more sensitive at high UVA dose. UVA-irradiated MR-1 survived better on tryptic soy agar than Luria-Bertani plates regardless of the growth stage. A 20% survival rate of MR-1 was observed following doses of 3.3 J of UVC m−2, 568 J of UVB m−2, 25 kJ of UVA m−2, and 558 J of solar UVB m−2, respectively. Photoreactivation conferred an increased survival rate to MR-1 of as much as 177- to 365-fold, 11- to 23-fold, and 3- to 10-fold following UVC, UVB, and solar light irradiation, respectively. A significant UV mutability to rifampin resistance was detected in both UVC- and UVB-treated samples, with the mutation frequency in the range of 10−5 to 10−6. Unlike in E. coli, the expression levels of the nucleotide excision repair (NER) component genes uvrA, uvrB, and uvrD were not damage inducible in MR-1. Complementation of Pseudomonas aeruginosa UA11079 (uvrA deficient) with uvrA of MR-1 increased the UVC survival of this strain by more than 3 orders of magnitude. Loss of damage inducibility of the NER system appears to contribute to the high sensitivity of this bacterium to UVR as well as to other DNA-damaging agents.
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McCready, S., and L. Marcello. "Repair of UV damage in Halobacterium salinarum." Biochemical Society Transactions 31, no. 3 (June 1, 2003): 694–98. http://dx.doi.org/10.1042/bst0310694.

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Halobacterium is one of the few known Archaea that tolerates high levels of sunlight in its natural environment. Photoreactivation is probably its most important strategy for surviving UV irradiation and we have shown that both of the major UV photoproducts, cyclobutane pyrimidine dimers (CPDs) and (6–4) photoproducts, can be very efficiently repaired by photoreactivation in this organism. There are two putative photolyase gene homologues in the published genome sequence of Halobacterium sp. NRC-1. We have made a mutant deleted in one of these, phr2, and confirmed that this gene codes for a CPD photolyase. (6–4) photoproducts are still photoreactivated in the mutant so we are currently establishing whether the other homologue, phr1, codes for a (6–4) photolyase. We have also demonstrated an excision repair capacity that operates in the absence of visible light but the nature of this pathway is not yet known. There is probably a bacteria-type excision-repair mechanism, since homologues of uvrA, uvrB, uvrC and uvrD have been identified in the Halobacterium genome. However, there are also homologues of eukaryotic nucleotide-excision-repair genes (Saccharomy cescerevisiae RAD3, RAD25 and RAD2) so there may be multiple repair mechanisms for UV damage in Halobacterium.
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42

Solis, James A., and Brad D. Rodgers. "Factors Affecting the Performance of New Oxygen Scavenging Polymer for Packaging Applications." Journal of Plastic Film & Sheeting 17, no. 4 (October 2001): 339–49. http://dx.doi.org/10.1106/22am-uvr8-x89x-7wbo.

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43

Allorent, Guillaume, Linnka Lefebvre-Legendre, Richard Chappuis, Marcel Kuntz, Thuy B. Truong, Krishna K. Niyogi, Roman Ulm, and Michel Goldschmidt-Clermont. "UV-B photoreceptor-mediated protection of the photosynthetic machinery inChlamydomonas reinhardtii." Proceedings of the National Academy of Sciences 113, no. 51 (December 5, 2016): 14864–69. http://dx.doi.org/10.1073/pnas.1607695114.

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Life on earth is dependent on the photosynthetic conversion of light energy into chemical energy. However, absorption of excess sunlight can damage the photosynthetic machinery and limit photosynthetic activity, thereby affecting growth and productivity. Photosynthetic light harvesting can be down-regulated by nonphotochemical quenching (NPQ). A major component of NPQ is qE (energy-dependent nonphotochemical quenching), which allows dissipation of light energy as heat. Photodamage peaks in the UV-B part of the spectrum, but whether and how UV-B induces qE are unknown. Plants are responsive to UV-B via the UVR8 photoreceptor. Here, we report in the green algaChlamydomonas reinhardtiithat UVR8 induces accumulation of specific members of the light-harvesting complex (LHC) superfamily that contribute to qE, in particular LHC Stress-Related 1 (LHCSR1) and Photosystem II Subunit S (PSBS). The capacity for qE is strongly induced by UV-B, although the patterns of qE-related proteins accumulating in response to UV-B or to high light are clearly different. The competence for qE induced by acclimation to UV-B markedly contributes to photoprotection upon subsequent exposure to high light. Our study reveals an anterograde link between photoreceptor-mediated signaling in the nucleocytosolic compartment and the photoprotective regulation of photosynthetic activity in the chloroplast.
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Thomas, D. C., M. Levy, and A. Sancar. "Amplification and purification of UvrA, UvrB, and UvrC proteins of Escherichia coli." Journal of Biological Chemistry 260, no. 17 (August 1985): 9875–83. http://dx.doi.org/10.1016/s0021-9258(17)39318-3.

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45

Tavridou, Eleni, Emanuel Schmid-Siegert, Christian Fankhauser, and Roman Ulm. "UVR8-mediated inhibition of shade avoidance involves HFR1 stabilization in Arabidopsis." PLOS Genetics 16, no. 5 (May 11, 2020): e1008797. http://dx.doi.org/10.1371/journal.pgen.1008797.

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46

Fernández, María Belén, Lorenzo Lamattina, and Raúl Cassia. "Functional analysis of the UVR8 photoreceptor from the monocotyledonous Zea mays." Plant Growth Regulation 92, no. 2 (June 25, 2020): 307–18. http://dx.doi.org/10.1007/s10725-020-00639-8.

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47

Rahden-Staroń, I., M. Szumiło, and P. Ziemkiewicz. "The effects of captan and captafol on different bacterial strains and on c-mitosis in V79 Chinese hamster fibroblasts." Acta Biochimica Polonica 41, no. 1 (March 31, 1994): 45–55. http://dx.doi.org/10.18388/abp.1994_4773.

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The mutagenic activity of captan and captafol was tested using Ames strains and strains showing an SOS response. Captafol was mutagenic in S. typhimurium strain TA102 (uvr+) and captan in strain TA104 (uvrB). Both captan and captafol elicit damages in DNA recognized by correndonuclease II, as shown by the repair test, and induced the SOS repair system in E. coli PQ37 (uvrA) strain. Only captafol induced the SOS system in PQ35 (uvr+). The lack of induction of beta-galactosidase at nonpermissive temperature in E. coli MD332 (dnaCs uvrA) strain showed that neither chemical was able to produce DNA breaks. In V79 Chinese hamster fibroblasts higher induction of c-mitosis by captafol than by captan (22% and 15% over the control, respectively) was accompanied by a higher decrease in nonprotein sulfhydryl groups, mainly GSH (41% and 77%, respectively). The content of protein sulfhydryl groups was decreased by either fungicide to a similar extent.
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48

Muthusamy, Muthusamy, Jin-A. Kim, and Soo-In Lee. "Phylogenomics-Based Reconstruction and Molecular Evolutionary Histories of Brassica Photoreceptor Gene Families." International Journal of Molecular Sciences 23, no. 15 (August 4, 2022): 8695. http://dx.doi.org/10.3390/ijms23158695.

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Photosensory proteins known as photoreceptors (PHRs) are crucial for delineating light environments in synchronization with other environmental cues and regulating their physiological variables in plants. However, this has not been well studied in the Brassica genus, which includes several important agricultural and horticultural crops. Herein, we identified five major PHR gene families—phytochrome (PHY), cryptochrome (CRY), phototropin (PHOT), F-box containing flavin binding proteins (ZTL/FKF1/LKP2), and UV RESISTANCE LOCUS 8 (UVR8)—genomic scales and classified them into subfamilies based on their phylogenetic clustering with Arabidopsis homologues. The molecular evolution characteristics of Brassica PHR members indicated indirect expansion and lost one to six gene copies at subfamily levels. The segmental duplication was possibly the driving force of the evolution and amplification of Brassica PHRs. Gene replication retention and gene loss events of CRY, PHY, and PHOT members found in diploid progenitors were highly conserved in their tetraploid hybrids. However, hybridization events were attributed to quantitative changes in UVR8 and ZTL/FKF1/LKP2 members. All PHR members underwent purifying selection. In addition, the transcript expression profiles of PHR genes in different tissue and in response to exogenous ABA, and abiotic stress conditions suggested their multiple biological significance. This study is helpful in understanding the molecular evolution characteristics of Brassica PHRs and lays the foundation for their functional characterization.
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Huang, Xi, Panyu Yang, Xinhao Ouyang, Liangbi Chen, and Xing Wang Deng. "Photoactivated UVR8-COP1 Module Determines Photomorphogenic UV-B Signaling Output in Arabidopsis." PLoS Genetics 10, no. 3 (March 20, 2014): e1004218. http://dx.doi.org/10.1371/journal.pgen.1004218.

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50

O’Hara, Andrew, and Gareth I. Jenkins. "In Vivo Function of Tryptophans in the Arabidopsis UV-B Photoreceptor UVR8." Plant Cell 24, no. 9 (September 2012): 3755–66. http://dx.doi.org/10.1105/tpc.112.101451.

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