UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii.
UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii.
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DOI：
10.1371/journal.pone.0051913
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发表时间：
2012
期刊：
影响因子：
3.7
通讯作者：
Rao BJ
中科院分区：
文献类型：
--
作者：
Shukla M;Minda R;Singh H;Tirumani S;Chary KV;Rao BJ
UVI 31+是进化上保守的BolA家族蛋白。在这项研究中，我们研究的存在，定位和可能的功能，这种蛋白质的背景下，单细胞衣藻，莱茵衣藻。C. reinhardtii表现出DNA内切酶活性，并且在UV胁迫下被诱导。此外，通常定位于细胞壁和蛋白核区域的UVI 31+在紫外线胁迫下重新分布到整个叶绿体内的点状焦点中，远离蛋白核。所观察到的诱导紫外线应力以及核酸内切酶活性表明这种蛋白质在DNA修复中的合理作用。我们还观察到UV ~（31+）在C. reinhardtii在黑暗条件下生长，由此蛋白质定位在蛋白核中增强。通过NMR研究纯化的类蛋白核和UVI 31+之间的生物分子相互作用表明蛋白质的无序环结构域参与其相互作用。
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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影响因子：
2.1
作者：
Koch, Birgit;Nybroe, Ole
通讯作者：
Nybroe, Ole
DOI：
10.1006/bbrc.1994.2043
发表时间：
1994-07-29
影响因子：
3.1
作者：
LEE, JK;PARK, EJ;PARK, SD
通讯作者：
PARK, SD
影响因子：
0.9
作者：
Rout, Ashok K.;Minda, R.;Chary, K. V. R.
通讯作者：
Chary, K. V. R.
影响因子：
8
作者：
Kasai, T;Inoue, M;Yokoyama, S
通讯作者：
Yokoyama, S
影响因子：
5.6
作者：
Schäfer, P;Scholz, SR;Meiss, G
通讯作者：
Meiss, G