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Title: Multiple Arabidopsis galacturonosyltransferases synthesize polymeric homogalacturonan by oligosaccharide acceptor‐dependent or de novo synthesis

Journal Article · · The Plant Journal
DOI: https://doi.org/10.1111/tpj.15640 · OSTI ID:1837461
 [1];  [2];  [3];  [3];  [2];  [3];  [2];  [2]; ORCiD logo [2]
  1. Complex Carbohydrate Research Center University of Georgia Athens GA 30602 USA, Department of Plant Biology University of Georgia Athens GA 30602 USA
  2. Complex Carbohydrate Research Center University of Georgia Athens GA 30602 USA, Department of Biochemistry and Molecular Biology University of Georgia Athens GA 30602 USA
  3. Complex Carbohydrate Research Center University of Georgia Athens GA 30602 USA

SUMMARY Homogalacturonan (HG), the most abundant pectic glycan, functions as a cell wall structural and signaling molecule essential for plant growth, development and response to pathogens. HG exists as a component of pectic homoglycans, heteroglycans and glycoconjugates. HG is synthesized by members of the GALACTURONOSYLTRANSFERASE (GAUT) family. UDP‐GalA‐dependent homogalacturonan:galacturonosyltransferase (HG:GalAT) activity has previously been demonstrated for GAUTs 1, 4 and 11, as well as the GAUT1:GAUT7 complex. Here, we show that GAUTs 10, 13 and 14 are also HG:GalATs and that GAUTs 1, 10, 11, 13, 14 and 1:7 synthesize polymeric HG in vitro . Comparison of the in vitro HG:GalAT specific activities of the heterologously‐expressed proteins demonstrates GAUTs 10 and 11 with the lowest, GAUT1 and GAUT13 with moderate, and GAUT14 and the GAUT1:GAUT7 complex with the highest HG:GalAT activity. GAUT13 and GAUT14 are also shown to de novo synthesize (initiate) HG synthesis in the absence of exogenous HG acceptors, an activity previously demonstrated for GAUT1:GAUT7. The rate of de novo HG synthesis by GAUT13 and GAUT14 is similar to their acceptor dependent HG synthesis, in contrast to GAUT1:GAUT7 for which de novo synthesis occurred at much lower rates than acceptor‐dependent synthesis. The results suggest a unique role for de novo HG synthesis by GAUTs 13 and 14. The reducing end of GAUT13‐ de novo‐ synthesized HG has covalently attached UDP, indicating that UDP‐GalA serves as both a donor and acceptor substrate during de novo HG synthesis. The functional significance of unique GAUT HG:GalAT catalytic properties in the synthesis of different pectin glycan or glycoconjugate structures is discussed.

Sponsoring Organization:
USDOE
OSTI ID:
1837461
Journal Information:
The Plant Journal, Journal Name: The Plant Journal Journal Issue: 6 Vol. 109; ISSN 0960-7412
Publisher:
Wiley-BlackwellCopyright Statement
Country of Publication:
United Kingdom
Language:
English

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