Nitric oxide-mediated regulation of the physiological and molecular responses induced by Ultraviolet-B (UV-B) radiation in plants

Fernández, María Belén; Latorre, Lucas; Lukaszewicz, Germán; Lamattina, Lorenzo; Cassia, Raúl

doi:10.1016/b978-0-12-818797-5.00017-0

Cited by 2 publications

(2 citation statements)

References 130 publications

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“…Photolyases transcript accumulation is induced upon UV-B exposition in several organisms, protecting them from cell death (An et al, 2021; Fernández et al, 2021, 2022; He et al, 2021). First, we analyzed the effect of UV-B (1.6 W m -2 ) on Synechococcus sp.…”

Section: Resultsmentioning

confidence: 99%

A bifunctional CPD/(6-4)- photolyase from the cyanobacteria Synechococcus sp. PCC 7335 constitutes an UV-B inducible operon: new insights into photolyases phylogenetic evolution

Fernández

Latorre

Correa‐Aragunde

et al. 2022

Preprint

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Photosynthetic organisms are continuously exposed to solar ultraviolet radiation-B (UV-B) because of their autotrophic lifestyle. UV-B provokes DNA damages, as cyclobutane pyrimidine dimers (CPD) or pyrimidine (6-4) pyrimidone photoproducts (6-4 PPs). The cryptochrome/photolyase family (CPF) comprises flavoproteins that are able to bind damaged or undamaged DNA. Photolyases (PHRs) are enzymes that repair either CPDs or 6-4 PPs. A natural bifunctional CPD/(6-4)- PHR (PhrSph98) was recently isolated from the UV-resistant bacteria Sphingomonas UV9. In this work, phylogenetic studies of bifunctional CPD/(6-4)- photolyases and its evolutionary relationship with other CPF members were performed. Amino acids involved in electron transfer and binding to FAD cofactor and DNA lesions were conserved in proteins from proteobacteria, planctomycete, bacteroidete, acidobacteria and cyanobacteria clades. Genome analysis revealed that the cyanobacteria Synechococcus sp. PCC 7335 encodes a two-gene assembly operon coding for a PHR and a bifunctional CPD/(6-4)- PHR. Operon structure was validated by RT-qPCR analysis and the polycistronic transcript accumulated after 15 minutes of UV-B irradiation. Conservation of structure and evolution is discussed. This is the first report of an UV-B inducible PHRs operon which encodes a CPD/(6-4)- photolyase with putative bifunctional role in the repair of CPDs and 6-4 PPs damages in oxygenic photosynthetic organisms.

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Section: Resultsmentioning

confidence: 99%

A bifunctional CPD/(6-4)- photolyase from the cyanobacteria Synechococcus sp. PCC 7335 constitutes an UV-B inducible operon: new insights into photolyases phylogenetic evolution

Fernández

Latorre

Correa‐Aragunde

et al. 2022

Preprint

Self Cite

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show abstract

“…Photolyases transcript accumulation is induced upon UV-B exposition in several organisms, protecting them from cell death (An et al, 2021;Fernández et al, 2021Fernández et al, , 2022He et al, 2021). First, we analyzed the effect of UV-B irradiation (1.6 W m −2 ) on Synechococcus sp.…”

Section: Phylogeny Of Cpf Proteinsmentioning

confidence: 99%

A putative bifunctional CPD/ (6-4) photolyase from the cyanobacteria Synechococcus sp. PCC 7335 is encoded by a UV-B inducible operon: New insights into the evolution of photolyases

Fernández

Latorre²,

Correa‐Aragunde³

et al. 2022

Front. Microbiol.

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Photosynthetic organisms are continuously exposed to solar ultraviolet radiation-B (UV-B) because of their autotrophic lifestyle. UV-B provokes DNA damage, such as cyclobutane pyrimidine dimers (CPD) or pyrimidine (6-4) pyrimidone photoproducts (6-4 PPs). The cryptochrome/photolyase family (CPF) comprises flavoproteins that can bind damaged or undamaged DNA. Photolyases (PHRs) are enzymes that repair either CPDs or 6-4 PPs. A natural bifunctional CPD/(6-4)- PHR (PhrSph98) was recently isolated from the UV-resistant bacteria Sphingomonas sp. UV9. In this work, phylogenetic studies of bifunctional CPD/(6-4)- photolyases and their evolutionary relationship with other CPF members were performed. Amino acids involved in electron transfer and binding to FAD cofactor and DNA lesions were conserved in proteins from proteobacteria, planctomycete, bacteroidete, acidobacteria and cyanobacteria clades. Genome analysis revealed that the cyanobacteria Synechococcus sp. PCC 7335 encodes a two-gene assembly operon coding for a PHR and a bifunctional CPD/(6-4) PHR- like. Operon structure was validated by RT-qPCR analysis and the polycistronic transcript accumulated after 15 min of UV-B irradiation. Conservation of structure and evolution is discussed. This study provides evidence for a UV-B inducible PHR operon that encodes a CPD/(6-4)- photolyase homolog with a putative bifunctional role in the repair of CPDs and 6-4 PPs damages in oxygenic photosynthetic organisms.

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Nitric oxide-mediated regulation of the physiological and molecular responses induced by Ultraviolet-B (UV-B) radiation in plants

Cited by 2 publications

References 130 publications

A bifunctional CPD/(6-4)- photolyase from the cyanobacteria Synechococcus sp. PCC 7335 constitutes an UV-B inducible operon: new insights into photolyases phylogenetic evolution

A bifunctional CPD/(6-4)- photolyase from the cyanobacteria Synechococcus sp. PCC 7335 constitutes an UV-B inducible operon: new insights into photolyases phylogenetic evolution

A putative bifunctional CPD/ (6-4) photolyase from the cyanobacteria Synechococcus sp. PCC 7335 is encoded by a UV-B inducible operon: New insights into the evolution of photolyases

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