Glucan synthase-like 2 is indispensable for paramylon synthesis in Euglena gracilis

FEBS Lett. 2017 May;591(10):1360-1370. doi: 10.1002/1873-3468.12659. Epub 2017 May 7.

Abstract

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.

Keywords: Euglena gracilis; paramylon; β-1,3-glucan synthase.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Euglena gracilis / genetics
  • Euglena gracilis / metabolism*
  • Gene Knockdown Techniques
  • Glucans / biosynthesis*
  • Glucosyltransferases / genetics*
  • Glucosyltransferases / metabolism
  • Phylogeny
  • Protozoan Proteins / metabolism
  • Uridine Diphosphate Glucose / metabolism

Substances

  • Glucans
  • Protozoan Proteins
  • paramylon
  • Glucosyltransferases
  • Uridine Diphosphate Glucose

Associated data

  • GENBANK/LC225614
  • GENBANK/LC225615
  • GENBANK/AAC48981
  • GENBANK/BAA21535
  • GENBANK/AAD37783
  • GENBANK/AAC49993
  • GENBANK/AAD11794
  • GENBANK/Q9AUE0
  • GENBANK/Q9SL03
  • GENBANK/OAO94775
  • GENBANK/Q9LTG5
  • GENBANK/Q3B724
  • GENBANK/Q9LYS6
  • GENBANK/Q9SHJ3
  • GENBANK/Q9LUD7
  • GENBANK/Q9SFU6
  • GENBANK/Q9SJM0
  • GENBANK/Q9S9U0
  • GENBANK/Q9ZT82
  • GENBANK/AAD25952
  • GENBANK/CUI14841
  • GENBANK/CUG05688