TY - JOUR
T1 - Glucan synthase-like 2 is indispensable for paramylon synthesis in Euglena gracilis
AU - Tanaka, Yuji
AU - Ogawa, Takahisa
AU - Maruta, Takanori
AU - Yoshida, Yuta
AU - Arakawa, Kazuharu
AU - Ishikawa, Takahiro
N1 - Funding Information:
This work was funded by the Core Research for Evolutional Science and Technology (CREST) Program “Creation of Basic Technology for Improved Bioenergy Production through Functional Analysis and Regulation of Algae and Other Aquatic Microorganisms” from the Japan Science and Technology Agency (JST), and supported in part by research funds from the Yamagata Prefectural Government and Tsuruoka City, Japan.
Publisher Copyright:
© 2017 Federation of European Biochemical Societies
PY - 2017/5/1
Y1 - 2017/5/1
N2 - The phytoflagellate Euglena gracilis produces a large amount of paramylon (PM), a conglomerate of liner β-1,3-glucan chains, as a storage polysaccharide. PM is synthesized from uridine diphosphate-glucose, but its mechanism of formation is largely unknown. Two enzymes, glucan synthase-like (EgGSL) 1 and EgGSL2 were previously identified as candidates for PM synthesis in a Euglena transcriptome analysis. Here, we performed a reverse genetic analysis on these enzymes. Knockdown of EgGSL2, but not EgGSL1, significantly inhibits PM accumulation in Euglena cells. Additionally, β-1,3-glucan synthesis is detected in a PM-associated membrane fraction extracted from Euglena cells. Our findings indicate that EgGSL2 is the predominant enzyme for PM biosynthesis.
AB - The phytoflagellate Euglena gracilis produces a large amount of paramylon (PM), a conglomerate of liner β-1,3-glucan chains, as a storage polysaccharide. PM is synthesized from uridine diphosphate-glucose, but its mechanism of formation is largely unknown. Two enzymes, glucan synthase-like (EgGSL) 1 and EgGSL2 were previously identified as candidates for PM synthesis in a Euglena transcriptome analysis. Here, we performed a reverse genetic analysis on these enzymes. Knockdown of EgGSL2, but not EgGSL1, significantly inhibits PM accumulation in Euglena cells. Additionally, β-1,3-glucan synthesis is detected in a PM-associated membrane fraction extracted from Euglena cells. Our findings indicate that EgGSL2 is the predominant enzyme for PM biosynthesis.
KW - Euglena gracilis
KW - paramylon
KW - β-1,3-glucan synthase
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U2 - 10.1002/1873-3468.12659
DO - 10.1002/1873-3468.12659
M3 - Article
C2 - 28423179
AN - SCOPUS:85019034217
SN - 0014-5793
VL - 591
SP - 1360
EP - 1370
JO - FEBS Letters
JF - FEBS Letters
IS - 10
ER -