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Plant Cell, Vol. 13, 755-768, April 2001, Copyright © 2001, American Society of Plant Physiologists
A Cell PlateSpecific Callose Synthase and Its Interaction with Phragmoplastin
Zonglie Hong,
Ashton J. Delauney, and
Desh Pal S. Verma
Department of Molecular Genetics and Plant Biotechnology Center, Ohio State University, 1060 Carmack Road, Columbus, Ohio 43210
Correspondence to:
Desh Pal S. Verma, verma.1{at}osu.edu (E-mail), 614-292-5379 (fax)
Callose is synthesized on the forming cell plate and several other locations in the plant. We cloned an Arabidopsis cDNA encoding a callose synthase (CalS1) catalytic subunit. The CalS1 gene comprises 42 exons with 41 introns and is transcribed into a 6.0-kb mRNA. The deduced peptide, with an approximate molecular mass of 226 kD, showed sequence homology with the yeast 1,3-ß-glucan synthases and is distinct from plant cellulose synthases. CalS1 contains 16 predicted transmembrane helices with the N-terminal region and a large central loop facing the cytoplasm. CalS1 interacts with two cell plateassociated proteins, phragmoplastin and a novel UDP-glucose transferase that copurifies with the CalS complex. That CalS1 is a cell platespecific enzyme is demonstrated by the observations that the green fluorescent proteinCalS1 fusion protein was localized at the growing cell plate, that expression of CalS1 in transgenic tobacco cells enhanced callose synthesis on the forming cell plate, and that these cell lines exhibited higher levels of CalS activity. These data also suggest that plant CalS may form a complex with UDP-glucose transferase to facilitate the transfer of substrate for callose synthesis.
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