期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 12, 页码 10793-10802出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.178020
关键词
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资金
- Austrian Science Fund [P19092, P20817]
- Gatsby Charitable Foundation
- Austrian Science Fund (FWF) [P20817, P19092] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [P 20817] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/E024874/1] Funding Source: researchfish
- BBSRC [BB/E024874/1] Funding Source: UKRI
Most plant glycoproteins contain substantial amounts of paucimannosidic N-glycans instead of their direct biosynthetic precursors, complex N-glycans with terminal N-acetylglucosamine residues. We now demonstrate that two beta-N-acetylhexosaminidases (HEXO1 and HEXO3) residing in different subcellular compartments jointly account for the formation of paucimannosidic N-glycans in Arabidopsis thaliana. Total N-glycan analysis of hexo knock-out plants revealed that HEXO1 and HEXO3 contribute equally to the production of paucimannosidic N-glycans in roots, whereas N-glycan processing in leaves depends more heavily on HEXO3 than on HEXO1. Because hexo1 hexo3 double mutants do not display any obvious phenotype even upon exposure to different forms of abiotic or biotic stress, it should be feasible to improve the quality of glycoprotein therapeutics produced in plants by down-regulation of endogenous beta-N-acetylhexosaminidase activities.
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