A gene required for the novel activation of a class II DNA photolyase in Chlamydomonas

Petersen, Jason L.; Small, Gary D.

doi:10.1093/nar/29.21.4472

Cited by 35 publications

(26 citation statements)

References 33 publications

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“…Chlamydomonas has CPD photorepair activity in both the chloroplast and nucleus (Small and Greimann, 1977), and its class II CPD photolyase is encoded by a single gene, PHR2 (Petersen et al, 1999). However, mutation of the PHR1 gene, which was discovered in mutagenesis experiments and has not been isolated yet, causes deficiencies in photorepair of both chloroplast and nuclear genes (Petersen and Small, 2001), suggesting that PHR1 acts through some unknown mechanism to regulate CPD photolyase.…”

Section: Discussionmentioning

confidence: 99%

The Native Cyclobutane Pyrimidine Dimer Photolyase of Rice Is Phosphorylated

Teranishi¹,

Nakamura²,

Morioka³

et al. 2008

Plant Physiol.

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The cyclobutane pyrimidine dimer (CPD) is a major type of DNA damage induced by ultraviolet B (UVB) radiation. CPD photolyase, which absorbs blue/UVA light as an energy source to monomerize dimers, is a crucial factor for determining the sensitivity of rice (Oryza sativa) to UVB radiation. Here, we purified native class II CPD photolyase from rice leaves. As the final purification step, CPD photolyase was bound to CPD-containing DNA conjugated to magnetic beads and then released by blue-light irradiation. The final purified fraction contained 54-and 56-kD proteins, whereas rice CPD photolyase expressed from Escherichia coli was a single 55-kD protein. Western-blot analysis using anti-rice CPD photolyase antiserum suggested that both the 54-and 56-kD proteins were the CPD photolyase. Treatment with protein phosphatase revealed that the 56-kD native rice CPD photolyase was phosphorylated, whereas the E. coli-expressed rice CPD photolyase was not. The purified native rice CPD photolyase also had significantly higher CPD photorepair activity than the E. coli-expressed CPD photolyase. According to the absorption, emission, and excitation spectra, the purified native rice CPD photolyase possesses both a pterin-like chromophore and an FAD chromophore. The binding activity of the native rice CPD photolyase to thymine dimers was higher than that of the E. coli-expressed CPD photolyase. These results suggest that the structure of the native rice CPD photolyase differs significantly from that of the E. coli-expressed rice CPD photolyase, and the structural modification of the native CPD photolyase leads to higher activity in rice.UVB radiation (280-320 nm) suppresses photosynthesis and protein biosynthesis, which in turn decreases growth and productivity (Teramura, 1983;Bornman and Teramura, 1993). UVB radiation also induces photodamage in DNA. The major UVB-induced lesions are cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone (6-4) photoproducts, which are formed between adjacent pyrimidines on the same strand (Britt, 1996). CPDs constitute the majority of these lesions (approximately 75%), and the (6-4) photoproducts account for the remainder. Such damage can be lethal or mutagenic to organisms and can also impede replication and transcription (Hoeijmakers, 2001;Sancar et al., 2004). Plants possess mechanisms to cope with UVB-induced DNA damage, including photoreactivation (photorepair) and nucleotide excision repair (also referred to as dark repair). In plants, photorepair is mediated by the enzyme photolyase, which absorbs blue/UVA light as an energy source to monomerize dimers and is the major pathway for counteracting UVB-induced DNA damage (Hidema et al., 1997;Britt, 1999). The sensitivity of rice (Oryza sativa) to UVB radiation varies among cultivars (Dai et al., 1992;Kumagai and Sato, 1992). We previously found that the CPD photorepair ability in UV-resistant rice is significantly higher than that in UV-sensitive rice and that this is due to an alteration of CPD photolyase activity resulting from spon...

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Section: Discussionmentioning

confidence: 99%

The Native Cyclobutane Pyrimidine Dimer Photolyase of Rice Is Phosphorylated

Teranishi¹,

Nakamura²,

Morioka³

et al. 2008

Plant Physiol.

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“…The Porphyra CRY that is most like plant CRYs is similar to a DNA photolyase (PHR2) (SI Appendix, Fig. 27 and Table S26) (57). In contrast, other red algae seem to encode plant CRYs; however, these group closely to the cyclobutane pyrimidine dimer class III photolyases (58) in some cases (SI Appendix, Fig.…”

Section: Significancementioning

confidence: 99%

Insights into the red algae and eukaryotic evolution from the genome of Porphyra umbilicalis (Bangiophyceae, Rhodophyta)

Brawley¹,

Blouin²,

Ficko-Blean³

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

228

222

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Porphyra umbilicalis (laver) belongs to an ancient group of red algae (Bangiophyceae), is harvested for human food, and thrives in the harsh conditions of the upper intertidal zone. Here we present the 87.7-Mbp haploid Porphyra genome (65.8% G + C content, 13,125 gene loci) and elucidate traits that inform our understanding of the biology of red algae as one of the few multicellular eukaryotic lineages. Novel features of the Porphyra genome shared by other red algae relate to the cytoskeleton, calcium signaling, the cell cycle, and stress-tolerance mechanisms including photoprotection. Cytoskeletal motor proteins in Porphyra are restricted to a small set of kinesins that appear to be the only universal cytoskeletal motors within the red algae. Dynein motors are absent, and most red algae, including Porphyra, lack myosin. This surprisingly minimal cytoskeleton offers a potential explanation for why red algal cells and multicellular structures are more limited in size than in most multicellular lineages. Additional discoveries further relating to the stress tolerance of bangiophytes include ancestral enzymes for sulfation of the hydrophilic galactan-rich cell wall, evidence for mannan synthesis that originated before the divergence of green and red algae, and a high capacity for nutrient uptake. Our analyses provide a comprehensive understanding of the red algae, which are both commercially important and have played a major role in the evolution of other algal groups through secondary endosymbioses.cytoskeleton | calcium-signaling | carbohydrate-active enzymes | stress tolerance | vitamin B 12T he red algae are one of the founding groups of photosynthetic eukaryotes (Archaeplastida) and among the few multicellular lineages within Eukarya. A red algal plastid, acquired through secondary endosymbiosis, supports carbon fixation, fatty acid synthesis, and other metabolic needs in many other algal groups in ways that are consequential. For example, diatoms and haptophytes have strong biogeochemical effects; apicomplexans cause human disease (e.g., malaria); and dinoflagellates include both coral symbionts and toxin-producing "red tides" (1). The evolutionary processes that produced the Archaeplastida and secondary algal lineages remain under investigation (2-5), but it is clear that both nuclear and plastid genes from the ancestral red algae have contributed dramatically to broader eukaryotic evolution and diversity. Consequently, the imprint of red algal metabolism on the Earth's climate system, aquatic foodwebs, and

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“…CPD photolyases are classified into two classes, I and II, based on amino acid sequence similarity (Yasui et al, 1994;Kanai et al, 1997;Todo, 1999). Class I photolyases are mostly found in bacteria and archea, whereas class II photolyases are found in some bacteria, archea, plants, green algae, insects, and vertebrates (Yasui et al, 1994;O'Connor et al, 1996;Ahmad et al, 1997;Petersen et al, 1999;Kim et al, 1996;Kato et al, 1994). Class I photolyases have generally two kinds of chromophore; reduced flavin-adenine dinucleotide (FAD) as a catalytic cofactor and either 8-hydroxy-5-deazaflavin or 5,10-methenyl tetrahydrofolate (MTHF) as a light harvesting factor (Sancar, 2003).…”

Section: Introductionmentioning

confidence: 99%

Biochemical and biological properties of DNA photolyases derived from utraviolet-sensitive rice cultivars

et al. 2007

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Class I and class II CPD photolyases are enzymes which repair pyrimidine dimers using visible light. A detailed characterization of class I CPD photolyases has been carried out, but little is known about the class II enzymes. Photolyases from rice are suitable for functional analyses because systematic breeding for long periods in Asian countries has led to the selection of naturally occurring mutations in the CPD photolyase gene. We report the biochemical characterization of rice mutant CPD photolyases purified as GST-form from Escherichia coli. We identified three amino acid changes, Gln126Arg, Gly255Ser, and Gln296His, among which Gln but not His at 296 is important for complementing phr-defective E. coli, binding UV-damage in E. coli, and binding thymine dimers in vitro. The photolyase with Gln at 296 has an apoenzyme:FAD ratio of 1 : 0.5 and that with His at 296 has an apoenzyme:FAD ratio of 1 : 0.12-0.25, showing a role for Gln at 296 in the binding of FAD not in the binding of thymine dimer. Concerning Gln or Arg at 126, the biochemical activity of the photolyases purified from E. coli and complementing activity for phr-defective E. coli are similarly proficient. However, the sensitivity to UV of cultivars differs depending on whether Gln or Arg is at 126. The role of Gln and Arg at 126 for photoreactivation in rice is discussed.

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A gene required for the novel activation of a class II DNA photolyase in Chlamydomonas

Cited by 35 publications

References 33 publications

The Native Cyclobutane Pyrimidine Dimer Photolyase of Rice Is Phosphorylated

The Native Cyclobutane Pyrimidine Dimer Photolyase of Rice Is Phosphorylated

Insights into the red algae and eukaryotic evolution from the genome of Porphyra umbilicalis (Bangiophyceae, Rhodophyta)

Biochemical and biological properties of DNA photolyases derived from utraviolet-sensitive rice cultivars

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