title: A novel mutation in KNOPF uncovers the role of alpha-glucosidase I during post-embryonic development in Arabidopsis thaliana.
abstract: N-glycosylation is a common protein modification. Joining of polypeptide and carbohydrate elements into hybrid molecules provides an opportunity to fine-tune protein properties. However, the role of N-glycosylation on the development of multicellular organisms remains elusive. Here we report a hypomorphic allele of KNOPF/GLUCOSIDASE 1, which allows us to describe the effects of impaired alpha-glucosidase I on post-embryonic development of plants for the first time. This knf-101 mutation alters cell shape but does not affect cell arrangements, except for the patterning of specialized epidermal cells, delineating the significance of N-glycan processing during epidermal development in Arabidopsis.
authors.affiliation: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
authors.forename: Chihiro
authors.initials: C
authors.lastname: Furumizu
authors.forename: Yoshibumi
authors.initials: Y
authors.lastname: Komeda
mesh_terms: D000483:Alleles; D017360:Arabidopsis / Q000166:cytology / Q000235:genetics / Q000254:growth & development*; D019521:Body Patterning / Q000235:genetics; D048430:Cell Shape; D009154:Mutation; D019441:Plant Epidermis / Q000166:cytology / Q000201:enzymology / Q000254:growth & development*; D018517:Plant Roots / Q000166:cytology / Q000235:genetics / Q000254:growth & development; D011134:Polysaccharides / Q000378:metabolism; D000520:alpha-Glucosidases / Q000235:genetics / Q000502:physiology*
chemical_list: D011134:Polysaccharides; C042059:glucosidase I; D000520:alpha-Glucosidases