A novel mutation in KNOPF uncovers the role of α-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 α-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.
Abbreviations: GUS, β-glucuronidase, RT-PCR, reverse transcription-PCR, 35S, cauliflower mosaic virus 35S RNA promoter, UTR, untranslated region
Keywords: Epidermal development, KNOPF/GLUCOSIDASE 1, N-glycan processing, α-Glucosidase I, Arabidopsis thaliana
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PII: S0014-5793(08)00421-3
doi:10.1016/j.febslet.2008.05.019
© 2008 Federation of European Biochemical Societies
