ArticlePloS one2012
UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 32 citations in OpenAlex.
- Extreme environmental adaptation mechanisms of Antarctic bryophytes are mainly the activation of antioxidants, secondary metabolites and photosynthetic pathways.BMC plant biology · 2023Article
- DNA-Specific DAPI Staining of the Pyrenoid Matrix During its Fission in Dunaliella salina (Dunal) Teodoresco (Chlorophyta).Current microbiology · 2020Article
- Structural characterization of a novel KH-domain containing plant chloroplast endonuclease.Scientific reports · 2018Article
- Article
- Pyrenoid loss in Chlamydomonas reinhardtii causes limitations in CO2 supply, but not thylakoid operating efficiency.Journal of experimental botany · 2017Article
- Structural and spectroscopic insights into BolA-glutaredoxin complexes.The Journal of biological chemistry · 2014Article
- Regulation of CCM genes in Chlamydomonas reinhardtii during conditions of light-dark cycles in synchronous cultures.Plant molecular biology · 2014Article
- ¹H, ¹³C and ¹⁵N resonance assignments of S114A mutant of UVI31+ from Chlamydomonas reinhardtii.Biomolecular NMR assignments · 2014Article
- Putative roles of glutaredoxin-BolA holo-heterodimers in plants.Plant signaling & behavior · 2014Article
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
UVI31+ is an evolutionarily conserved BolA family protein. In this study we examine the presence, localization and possible functions of this protein in the context of a unicellular alga, Chlamydomonas reinhardtii. UVI31+ in C. reinhardtii exhibits DNA endonuclease activity and is induced upon UV stress. Further, UVI31+ that normally localizes to the cell wall and pyrenoid regions gets redistributed into punctate foci within the whole chloroplast, away from the pyrenoid, upon UV stress. The observed induction upon UV-stress as well as the endonuclease activity suggests plausible role of this protein in DNA repair. We have also observed that UV31+ is induced in C. reinhardtii grown in dark conditions, whereby the protein localization is enhanced in the pyrenoid. Biomolecular interaction between the purified pyrenoids and UVI31+ studied by NMR demonstrates the involvement of the disordered loop domain of the protein in its interaction.
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