Increase in the amount of celA1 protein in tobacco [Nicotiana tabacum] BY-2 cells by a cellulose biosynthesis inhibitor, 2,6-dichlorobenzonitrile

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 celA1 gene was cloned from cotton fiber, and this gene was identified from the rsw1 mutant of Arabidopsis as a cataly...

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Bibliographic Details
Published inPlant and cell physiology Vol. 39; no. 7; pp. 779 - 785
Main Authors Nakagawa, N. (Hiroshima Univ. (Japan). Faculty of Integrated Arts and Sciences), Sakurai, N
Format Journal Article
LanguageEnglish
Published Oxford Oxford University Press 01.07.1998
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Summary: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 celA1 gene was cloned from cotton fiber, and this gene was identified from the rsw1 mutant of Arabidopsis as a catalytic subunit of cellulose synthase. The cloning of these genes enables us to obtain specific antibodies against cellulose synthase. A highly specific antibody against celA1 protein was prepared and used to detect the protein from microsomal fraction of tobacco BY-2 cells. The quantity of celA1 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 mu-M DCB (a specific inhibitor of cellulose biosynthesis) produced 1/10 of cellulose content of the normal cells, but had much more celA1 protein than the normal cells. The amount of polysaccharides in the EDTA-soluble fraction was relatively increased in habituated cells. The results suggest that celA1 protein is stabilized upon DCB binding and that the crystallization of cellulose microfibrils is inhibited simultaneously
Bibliography:F61
H50
1998007697
ark:/67375/HXZ-4TZKNMML-L
1 To whom correspondence should be addressed.
istex:F8388E8BE97514A46A90B2796CB53E26B045173E
ArticleID:39.7.779
ISSN:0032-0781
1471-9053
DOI:10.1093/oxfordjournals.pcp.a029434