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

Autor: Srikanth Tirumani, Renu Minda, Basuthkar J. Rao, Manish Shukla, Kandala V. R. Chary, Himanshu Singh
Rok vydání: 2012
Předmět:
Chloroplasts
Chlamydomonas reinhardtii
lcsh:Medicine
Plant Science
Biochemistry
Physical Chemistry
Pyrenoid
Endonuclease
Molecular cell biology
Cell Wall
Gene Expression Regulation
Plant
lcsh:Science
Plant Proteins
Cellular Stress Responses
Chlamydomonas Reinhardtii
Multidisciplinary
biology
Applied Chemistry
Darkness
Protein subcellular localization prediction
Recombinant Proteins
Signaling Cascades
Transport protein
Cell biology
Chloroplast
Nucleic acids
Protein Transport
Chemistry
Research Article
Signal Transduction
Ultraviolet Rays
Plant Cell Biology
Nuclear Magnetic Resonance
Protein domain
Biophysics
DNA repair
Stress Signaling Cascade
Model Organisms
Plant and Algal Models
Deoxyribonuclease I
Protein Interaction Domains and Motifs
Biology
lcsh:R
DNA
biology.organism_classification
Molecular biology
Enzyme Activation
Chemical Properties
biology.protein
lcsh:Q
Zdroj: PLoS ONE
PLoS ONE, Vol 7, Iss 12, p e51913 (2012)
ISSN: 1932-6203
Popis: 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.
Databáze: OpenAIRE
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