Matches in SemOpenAlex for { <https://semopenalex.org/work/W2891174720> ?p ?o ?g. }
- W2891174720 abstract "Abstract Chlamydomonas reinhardtii is a single celled alga that undergoes apoptosis in response to UV-C irradiation. UVI31+, a novel UV-inducible DNA endonuclease in C . reinhardtii , which normally localizes near cell wall and pyrenoid regions, gets redistributed into punctate foci within the whole chloroplast, away from the pyrenoid, upon UV-stress. Solution NMR structure of the first putative UV inducible endonuclease UVI31+ revealed an α 1 –β 1 –β 2 –α 2 –α 3 –β 3 fold similar to BolA and type II KH-domain ubiquitous protein families. Three α−helices of UVI31+ constitute one side of the protein surface, which are packed to the other side, made of three-stranded β–sheet, with intervening hydrophobic residues. A twenty-three residues long polypeptide stretch (D54-H76) connecting β 1 and β 2 strands is found to be highly flexible. Interestingly, UVI31+ recognizes the DNA primarily through its β–sheet. We propose that the catalytic triad residues involving Ser114, His95 and Thr116 facilitate DNA endonuclease activity of UVI31+. Further, decreased endonuclease activity of the S114A mutant is consistent with the direct participation of Ser114 in the catalysis. This study provides the first structural description of a plant chloroplast endonuclease that is regulated by UV-stress response." @default.
- W2891174720 created "2018-09-27" @default.
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- W2891174720 date "2018-09-13" @default.
- W2891174720 modified "2023-10-09" @default.
- W2891174720 title "Structural characterization of a novel KH-domain containing plant chloroplast endonuclease" @default.
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- W2891174720 doi "https://doi.org/10.1038/s41598-018-31142-w" @default.
- W2891174720 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6137056" @default.
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