UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii.
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 st...
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Public Library of Science (PLoS)
2012-01-01
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Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3524116?pdf=render |
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author | Manish Shukla Renu Minda Himanshu Singh Srikanth Tirumani Kandala V R Chary Basuthkar J Rao |
author_facet | Manish Shukla Renu Minda Himanshu Singh Srikanth Tirumani Kandala V R Chary Basuthkar J Rao |
author_sort | Manish Shukla |
collection | DOAJ |
description | 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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language | English |
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spelling | doaj.art-21b93453ca5b4bf6af949af02ddc14c92022-12-21T19:10:43ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-01712e5191310.1371/journal.pone.0051913UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii.Manish ShuklaRenu MindaHimanshu SinghSrikanth TirumaniKandala V R CharyBasuthkar J RaoUVI31+ 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.http://europepmc.org/articles/PMC3524116?pdf=render |
spellingShingle | Manish Shukla Renu Minda Himanshu Singh Srikanth Tirumani Kandala V R Chary Basuthkar J Rao UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii. PLoS ONE |
title | UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii. |
title_full | UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii. |
title_fullStr | UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii. |
title_full_unstemmed | UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii. |
title_short | UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii. |
title_sort | uvi31 is a dna endonuclease that dynamically localizes to chloroplast pyrenoids in c reinhardtii |
url | http://europepmc.org/articles/PMC3524116?pdf=render |
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