Journal Article

Increase in the Amount of celA1 Protein in Tobacco BY-2 Cells by a Cellulose Biosynthesis Inhibitor, 2,6-dichlorobenzonitrile

Naoki Nakagawa and Naoki Sakurai

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 39, issue 7, pages 779-785
Published in print July 1998 | ISSN: 0032-0781
Published online July 1998 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029434
Increase in the Amount of celA1 Protein in Tobacco BY-2 Cells by a Cellulose Biosynthesis Inhibitor, 2,6-dichlorobenzonitrile

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The biochemical analysis of cellulose biosynthesis by plants has been a difficult problem due to the lack of a reliable assay procedure for cellulose synthase activity. Recently, the celAl gene was cloned from cotton fiber, and this gene was identified from the rsw1 mutant of Arabidopsis as a catalytic subunit of cellulose synthase (Arioli et al. 1998). The cloning of these genes enables us to obtain specific antibodies against cellulose synthase. A highly specific antibody against celAl protein was prepared and used to detect the protein from microsomal fraction of tobacco BY-2 cells. The quantity of celAl protein in microsomal fraction of normal BY-2 cells was under the detection limit, although they contained a large quantity of cellulose. In contrast, cells habituated to 1 μM DCB (a specific inhibitor of cellulose biosynthesis) produced 1/10 of cellulose content of the normal cells, but had much more celAl protein than the normal cells. The amount of polysaccharides in the EDTA-soluble fraction was relatively increased in habituated cells. The results suggest that celAl protein is stabilized upon DCB binding and that the crystallization of cellulose microfibrils is inhibited simultaneously.

Keywords: Anti-peptide antibody; celAl gene; Cellulose; 2,6-Dichlorobenzonitrile; Nicotiana tabacum BY-2; RSW1

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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