UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii

Manish Shukla; Renu Minda; Himanshu Singh; Srikanth Tirumani; Kandala V R Chary; Basuthkar J Rao

doi:10.1371/journal.pone.0051913

UVI31+ is a DNA endonuclease that dynamically localizes to chloroplast pyrenoids in C. reinhardtii

PLoS One. 2012;7(12):e51913. doi: 10.1371/journal.pone.0051913. Epub 2012 Dec 17.

Authors

Manish Shukla¹, Renu Minda, Himanshu Singh, Srikanth Tirumani, Kandala V R Chary, Basuthkar J Rao

Affiliation

¹ Department of Biological Sciences, Tata Institute of Fundamental Research, Colaba, Mumbai, India.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cell Wall / metabolism
Chlamydomonas reinhardtii / enzymology*
Chlamydomonas reinhardtii / genetics
Chlamydomonas reinhardtii / metabolism
Chloroplasts / enzymology*
Chloroplasts / metabolism
Darkness
Deoxyribonuclease I / chemistry
Deoxyribonuclease I / genetics
Deoxyribonuclease I / isolation & purification
Deoxyribonuclease I / metabolism*
Enzyme Activation
Gene Expression Regulation, Plant
Plant Proteins / metabolism*
Protein Interaction Domains and Motifs
Protein Transport
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / isolation & purification
Recombinant Proteins / metabolism
Ultraviolet Rays

Substances

Plant Proteins
Recombinant Proteins
Deoxyribonuclease I

Grants and funding

This work was funded by Department of Atomic Energy at TIFR. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.