Diatom Vacuolar 1,6-β-Transglycosylases can Functionally Complement the Respective Yeast Mutants

The Journal of Eukaryotic Microbiology
Weichao HuangPeter G Kroth

Abstract

Diatoms are unicellular photoautotrophic algae, which can be found in any aquatic habitat. The main storage carbohydrate of diatoms is chrysolaminarin, a nonlinear β-glucan, consisting of a linear 1,3-β-chain with 1,6-β-branches, which is stored in cytoplasmic vacuoles. The metabolic pathways of chrysolaminarin synthesis in diatoms are poorly investigated, therefore we studied two potential 1,6-β-transglycosylases (TGS) of the diatom Phaeodactylum tricornutum which are similar to yeast Kre6 proteins and which potentially are involved in the branching of 1,3-β-glucan chains by adding d-glucose as 1,6-side chains. We genetically fused the full-length diatom TGS proteins to GFP and expressed these constructs in P. tricornutum, demonstrating that the enzymes are apparently located in the vacuoles, which indicates that branching of chrysolaminarin may occur in these organelles. Furthermore, we demonstrated the functionality of the diatom enzymes by expressing TGS1 and 2 proteins in yeast, which resulted in a partial complementation of growth deficiencies of a transglycosylase-deficient ∆kre6 yeast strain.

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Citations

Jul 19, 2017·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Ansgar Gruber, Peter G Kroth
Jul 19, 2017·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Weichao Huang, Fayza Daboussi
Mar 31, 2018·Applied Microbiology and Biotechnology·Hirofumi UchiyamaEnoch Y Park
Apr 20, 2018·Proceedings of the National Academy of Sciences of the United States of America·Weichao HuangPeter G Kroth
Apr 14, 2017·Applied Microbiology and Biotechnology·Aubrey DavisMark Hildebrand
Jan 26, 2020·Trends in Biotechnology·Thomas ButlerSeetharaman Vaidyanathan
Mar 23, 2021·Frontiers in Plant Science·Malika ChabiUgo Cenci

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