Document Detail


A novel mutation in KNOPF uncovers the role of alpha-glucosidase I during post-embryonic development in Arabidopsis thaliana.
MedLine Citation:
PMID:  18503769     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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:
Chihiro Furumizu; Yoshibumi Komeda
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-05-27
Journal Detail:
Title:  FEBS letters     Volume:  582     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-06-16     Completed Date:  2008-08-25     Revised Date:  2009-06-08    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  2237-41     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
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MeSH Terms
Descriptor/Qualifier:
Alleles
Arabidopsis / cytology,  genetics,  growth & development*
Body Patterning / genetics
Cell Shape
Mutation*
Plant Epidermis / cytology,  enzymology,  growth & development*
Plant Roots / cytology,  genetics,  growth & development
Polysaccharides / metabolism
alpha-Glucosidases / genetics,  physiology*
Chemical
Reg. No./Substance:
0/Polysaccharides; EC 3.2.1.-/glucosidase I; EC 3.2.1.20/alpha-Glucosidases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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