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α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
Novel mutations in the RSW1 and KNOPF genes were identified in a large-scale screen for mutations that affect cell expansion in early Arabidopsis embryos. Embryos from both types of mutants were radially swollen with greatly reduced levels of crystalline cellulose, the principal structural component...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2002
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173474/ https://www.ncbi.nlm.nih.gov/pubmed/11901167 http://dx.doi.org/10.1083/jcb.200111093 |
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author | Gillmor, C. Stewart Poindexter, Patricia Lorieau, Justin Palcic, Monica M. Somerville, Chris |
author_facet | Gillmor, C. Stewart Poindexter, Patricia Lorieau, Justin Palcic, Monica M. Somerville, Chris |
author_sort | Gillmor, C. Stewart |
collection | PubMed |
description | Novel mutations in the RSW1 and KNOPF genes were identified in a large-scale screen for mutations that affect cell expansion in early Arabidopsis embryos. Embryos from both types of mutants were radially swollen with greatly reduced levels of crystalline cellulose, the principal structural component of the cell wall. Because RSW1 was previously shown to encode a catalytic subunit of cellulose synthase, the similar morphology of knf and rsw1-2 embryos suggests that the radially swollen phenotype of knf mutants is largely due to their cellulose deficiency. Map-based cloning of the KNF gene and enzyme assays of knf embryos demonstrated that KNF encodes α-glucosidase I, the enzyme that catalyzes the first step in N-linked glycan processing. The strongly reduced cellulose content of knf mutants indicates that N-linked glycans are required for cellulose biosynthesis. Because cellulose synthase catalytic subunits do not appear to be N glycosylated, the N-glycan requirement apparently resides in other component(s) of the cellulose synthase machinery. Remarkably, cellular processes other than extracellular matrix biosynthesis and the formation of protein storage vacuoles appear unaffected in knf embryos. Thus in Arabidopsis cells, like yeast, N-glycan trimming is apparently required for the function of only a small subset of N-glycoproteins. |
format | Text |
id | pubmed-2173474 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21734742008-05-01 α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis Gillmor, C. Stewart Poindexter, Patricia Lorieau, Justin Palcic, Monica M. Somerville, Chris J Cell Biol Article Novel mutations in the RSW1 and KNOPF genes were identified in a large-scale screen for mutations that affect cell expansion in early Arabidopsis embryos. Embryos from both types of mutants were radially swollen with greatly reduced levels of crystalline cellulose, the principal structural component of the cell wall. Because RSW1 was previously shown to encode a catalytic subunit of cellulose synthase, the similar morphology of knf and rsw1-2 embryos suggests that the radially swollen phenotype of knf mutants is largely due to their cellulose deficiency. Map-based cloning of the KNF gene and enzyme assays of knf embryos demonstrated that KNF encodes α-glucosidase I, the enzyme that catalyzes the first step in N-linked glycan processing. The strongly reduced cellulose content of knf mutants indicates that N-linked glycans are required for cellulose biosynthesis. Because cellulose synthase catalytic subunits do not appear to be N glycosylated, the N-glycan requirement apparently resides in other component(s) of the cellulose synthase machinery. Remarkably, cellular processes other than extracellular matrix biosynthesis and the formation of protein storage vacuoles appear unaffected in knf embryos. Thus in Arabidopsis cells, like yeast, N-glycan trimming is apparently required for the function of only a small subset of N-glycoproteins. The Rockefeller University Press 2002-03-18 /pmc/articles/PMC2173474/ /pubmed/11901167 http://dx.doi.org/10.1083/jcb.200111093 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Gillmor, C. Stewart Poindexter, Patricia Lorieau, Justin Palcic, Monica M. Somerville, Chris α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis |
title | α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
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title_full | α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
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title_fullStr | α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
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title_full_unstemmed | α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
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title_short | α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
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title_sort | α-glucosidase i is required for cellulose biosynthesis and morphogenesis in arabidopsis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173474/ https://www.ncbi.nlm.nih.gov/pubmed/11901167 http://dx.doi.org/10.1083/jcb.200111093 |
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