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Title: Identification of xylan arabinosyl 2-O-xylosyltransferases catalyzing the addition of 2-O-xylosyl residue onto arabinosyl side chains of xylan in grass species

Journal Article · · The Plant Journal
DOI: https://doi.org/10.1111/tpj.15939 · OSTI ID:2418959
 [1];  [2];  [3];  [4];  [4];  [2];  [2]; ORCiD logo [4]
  1. Univ. of Georgia, Athens, GA (United States); OSTI
  2. Kyung Hee Univ., Yongin (Korea, Republic of)
  3. Harvard Univ., Cambridge, MA (United States)
  4. Univ. of Georgia, Athens, GA (United States)
+ Show Author Affiliations

Grass xylan, the major hemicellulose in both primary and secondary cell walls, is heavily decorated with α-1,3-linked arabinofuranosyl (Araf) residues that may be further substituted at O-2 with xylosyl (Xyl) or Araf residues. Although xylan 3-O-arabinosyltransferases (XATs) catalyzing 3-O-Araf addition onto xylan have been characterized, glycosyltransferases responsible for the transfer of 2-O-Xyl or 2-O-Araf onto 3-O-Araf residues of xylan to produce the Xyl-Araf and Araf-Araf disaccharide side chains remain to be identified. In this report, we showed that a rice GT61 member, named OsXAXT1 (xylan arabinosyl 2-O-xylosyltransferase 1) herein, was able to mediate the addition of Xyl-Araf disaccharide side chains onto xylan when heterologously co-expressed with OsXAT2 in the Arabidopsis gux1/2/3 (glucuronic acid substitution of xylan 1/2/3) triple mutant that lacks any glycosyl substitutions. Recombinant OsXAXT1 protein expressed in human embryonic kidney 293 cells exhibited a xylosyltransferase activity catalyzing the addition of Xyl from UDP-Xyl onto arabinosylated xylooligomers. Further, consistent with its function as a xylan arabinosyl 2-O-xylosyltransferase, CRISPR-Cas9-mediated mutations of the OsXAXT1 gene in transgenic rice plants resulted in a reduction in the level of Xyl-Araf disaccharide side chains in xylan. Furthermore, we revealed that XAXT1 close homologs from several other grass species, including switchgrass, maize, and Brachypodium, possessed the same functions as OsXAXT1, indicating functional conservation of XAXTs in grass species. Together, our findings establish that grass XAXTs are xylosyltransferases catalyzing Xyl transfer onto O-2 of Araf residues of xylan to form the Xyl-Araf disaccharide side chains, which furthers our understanding of genes involved in xylan biosynthesis.

Research Organization:
Univ. of Georgia, Athens, GA (United States)
Sponsoring Organization:
National Research Foundation of Korea (NRF); USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
FG02-03ER15415
OSTI ID:
2418959
Journal Information:
The Plant Journal, Journal Name: The Plant Journal Journal Issue: 1 Vol. 112; ISSN 0960-7412
Publisher:
Society for Experimental BiologyCopyright Statement
Country of Publication:
United States
Language:
English

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59 BASIC BIOLOGICAL SCIENCES
GT61
XAT
XAXT
cell wall
grass
xylan
xylosyltransferase