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A gene from the cellulose synthase-like C family encodes a beta-1,4 glucan synthase.
Cocuron, Jean-Christophe; Lerouxel, Olivier; Drakakaki, Georgia; Alonso, Ana P; Liepman, Aaron H; Keegstra, Kenneth; Raikhel, Natasha; Wilkerson, Curtis G.
Afiliación
  • Cocuron JC; Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.
Proc Natl Acad Sci U S A ; 104(20): 8550-5, 2007 May 15.
Article en En | MEDLINE | ID: mdl-17488821
Despite the central role of xyloglucan (XyG) in plant cell wall structure and function, important details of its biosynthesis are not understood. To identify the gene(s) responsible for synthesizing the beta-1,4 glucan backbone of XyG, we exploited a property of nasturtium (Tropaeolum majus) seed development. During the last stages of nasturtium seed maturation, a large amount of XyG is deposited as a reserve polysaccharide. A cDNA library was produced from mRNA isolated during the deposition of XyG, and partial sequences of 10,000 cDNA clones were determined. A single member of the C subfamily from the large family of cellulose synthase-like (CSL) genes was found to be overrepresented in the cDNA library. Heterologous expression of this gene in the yeast Pichia pastoris resulted in the production of a beta-1,4 glucan, confirming that the CSLC protein has glucan synthase activity. The Arabidopsis CSLC4 gene, which is the gene with the highest sequence similarity to the nasturtium CSL gene, is coordinately expressed with other genes involved in XyG biosynthesis. These and other observations provide a compelling case that the CSLC gene family encode proteins that synthesize the XyG backbone.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Genes de Plantas / Tropaeolum / Glucosiltransferasas Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2007 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Genes de Plantas / Tropaeolum / Glucosiltransferasas Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2007 Tipo del documento: Article País de afiliación: Estados Unidos