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Title: Bifunctional glycosyltransferases catalyze both extension and termination of pectic galactan oligosaccharides

Journal Article · · The Plant Journal
DOI:https://doi.org/10.1111/tpj.13860· OSTI ID:1429122
ORCiD logo [1];  [1];  [1];  [1];  [2]; ORCiD logo [1]; ORCiD logo [3]
  1. Joint BioEnergy Institute and Environmental Genomics and Systems Biology Division Lawrence Berkeley National Laboratory Berkeley CA 94702 USA
  2. Department of Chemistry Center for Nanomedicine and Theranostics Technical University of Denmark DK‐2800 Kongens Lyngby Denmark
  3. Joint BioEnergy Institute and Environmental Genomics and Systems Biology Division Lawrence Berkeley National Laboratory Berkeley CA 94702 USA, Department of Plant and Microbial Biology University of California Berkeley CA 94720 USA

Summary Pectins are the most complex polysaccharides of the plant cell wall. Based on the number of methylations, acetylations and glycosidic linkages present in their structures, it is estimated that up to 67 transferase activities are involved in pectin biosynthesis. Pectic galactans constitute a major part of pectin in the form of side‐chains of rhamnogalacturonan‐I. In Arabidopsis, galactan synthase 1 (GALS1) catalyzes the addition of galactose units from UDP‐Gal to growing β‐1,4‐galactan chains. However, the mechanisms for obtaining varying degrees of polymerization remain poorly understood. In this study, we show that At GALS1 is bifunctional, catalyzing both the transfer of galactose from UDP‐α‐ d ‐Gal and the transfer of an arabinopyranose from UDP‐β‐ l ‐Ara p to galactan chains. The two substrates share a similar structure, but UDP‐α‐ d ‐Gal is the preferred substrate, with a 10‐fold higher affinity. Transfer of Ara p to galactan prevents further addition of galactose residues, resulting in a lower degree of polymerization. We show that this dual activity occurs both in vitro and in vivo . The herein described bifunctionality of At GALS1 may suggest that plants can produce the incredible structural diversity of polysaccharides without a dedicated glycosyltransferase for each glycosidic linkage.

Sponsoring Organization:
USDOE
OSTI ID:
1429122
Journal Information:
The Plant Journal, Journal Name: The Plant Journal Vol. 94 Journal Issue: 2; ISSN 0960-7412
Publisher:
Wiley-BlackwellCopyright Statement
Country of Publication:
United Kingdom
Language:
English
Citation Metrics:
Cited by: 20 works
Citation information provided by
Web of Science

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