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Conservation of endo -glucanase 16 (EG16) activity across highly divergent plant lineages

Journal Article · · Biochemical Journal
DOI:https://doi.org/10.1042/bcj20210341· OSTI ID:1850708
 [1];  [1];  [2];  [2];  [3]
  1. Michael Smith Laboratories, University of British Columbia, 2185 East Mall, Vancouver, BC Canada V6T 1Z1; Department of Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Life Sciences Centre, Vancouver, BC, Canada V6T 1Z3
  2. Department of Biology, Pennsylvania State University, 208 Mueller Laboratory, University Park, PA 16802, U.S.A.
  3. Michael Smith Laboratories, University of British Columbia, 2185 East Mall, Vancouver, BC Canada V6T 1Z1; Department of Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Life Sciences Centre, Vancouver, BC, Canada V6T 1Z3; Department of Botany, University of British Columbia, 3200-6270 University Blvd., Vancouver, BC, Canada V6H 1Z4; Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, Canada V6T 1Z1
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Plant cell walls are highly dynamic structures that are composed predominately of polysaccharides. As such, endogenous carbohydrate active enzymes (CAZymes) are central to the synthesis and subsequent modification of plant cells during morphogenesis. The endo-glucanase 16 (EG16) members constitute a distinct group of plant CAZymes, angiosperm orthologs of which were recently shown to have dual β-glucan/xyloglucan hydrolase activity. Molecular phylogeny indicates that EG16 members comprise a sister clade with a deep evolutionary relationship to the widely studied apoplastic xyloglucan endo-transglycosylases/hydrolases (XTH). A cross-genome survey indicated that EG16 members occur as a single ortholog across species and are widespread in early diverging plants, including the non-vascular bryophytes, for which functional data were previously lacking. Remarkably, enzymological characterization of an EG16 ortholog from the model moss Physcomitrella patens (PpEG16) revealed that EG16 activity and sequence/structure are highly conserved across 500 million years of plant evolution, vis-à-vis orthologs from grapevine and poplar. Ex vivo biomechanical assays demonstrated that the application of EG16 gene products caused abrupt breakage of etiolated hypocotyls rather than slow extension, thereby indicating a mode-of-action distinct from endogenous expansins and microbial endo-glucanases. The biochemical data presented here will inform future genomic, genetic, and physiological studies of EG16 enzymes.

Research Organization:
Pennsylvania State Univ., University Park, PA (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
DOE Contract Number:
SC0001090
OSTI ID:
1850708
Journal Information:
Biochemical Journal, Vol. 478, Issue 16; ISSN 0264-6021
Publisher:
Biochemical Society
Country of Publication:
United States
Language:
English

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