NDLI: Enzymatic Properties and Subcellular Localization of Arabidopsis β-N-Acetylhexosaminidases1 [W] [OA]

Content Provider	PubMed Central
Author	Strasser, Richard Singh, Bondili Jayakumar Jennifer, Schoberer Svoboda, Barbara Eva, Liebminger Josef, Glössl Altmann, Friedrich Steinkellner, Herta Mach, Lukas
Abstract	Plant glycoproteins contain substantial amounts of paucimannosidic N-glycans lacking terminal GlcNAc residues at their nonreducing ends. It has been proposed that this is due to the action of β-hexosaminidases during late stages of N-glycan processing or in the course of N-glycan turnover. We have now cloned the three putative β-hexosaminidase sequences present in the Arabidopsis (Arabidopsis thaliana) genome. When heterologously expressed as soluble forms in Spodoptera frugiperda cells, the enzymes (termed HEXO1–3) could all hydrolyze the synthetic substrates p-nitrophenyl-2-acetamido-2-deoxy-β-d-glucopyranoside, p-nitrophenyl-2-acetamido-2-deoxy-β-d-galactopyranoside, 4-methylumbelliferyl-2-acetamido-2-deoxy-β-d-glucopyranoside, and 4-methylumbelliferyl-6-sulfo-2-acetamido-2-deoxy-β-d-glucopyranoside, albeit to a varying extent. HEXO1 to HEXO3 were further able to degrade pyridylaminated chitotriose, whereas pyridylaminated chitobiose was only cleaved by HEXO1. With N-glycan substrates, HEXO1 displayed a much higher specific activity than HEXO2 and HEXO3. Nevertheless, all three enzymes were capable of removing terminal GlcNAc residues from the α1,3- and α1,6-mannosyl branches of biantennary N-glycans without any strict branch preference. Subcellular localization studies with HEXO-fluorescent protein fusions transiently expressed in Nicotiana benthamiana plants showed that HEXO1 is a vacuolar protein. In contrast, HEXO2 and HEXO3 are mainly located at the plasma membrane. These results indicate that HEXO1 participates in N-glycan trimming in the vacuole, whereas HEXO2 and/or HEXO3 could be responsible for the processing of N-glycans present on secretory glycoproteins.
Related Links	http://dx.doi.org/10.1104/pp.107.101162
Ending Page	16
Page Count	12
Starting Page	5
File Format	PDF
ISSN	00320889
e-ISSN	15322548
Journal	Plant Physiology
Issue Number	1
Volume Number	145
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2007-07-01
Access Restriction	Open
Rights Holder	American Society of Plant Biologists
Subject Keyword	Plant Science Genetics Physiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Physiology Plant Science

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