Structural characterization of a novel KH-domain containing plant chloroplast endonuclease.

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 α₁-β₁-β₂-α₂-α₃-β₃ 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 polyp

SUBMITTER: Rout AK 

PROVIDER: S-EPMC6137056 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature