Journal article
Plant callose synthase complexes
Plant molecular biology, Vol.47(6), pp.693-701
12/2001
Handle:
https://hdl.handle.net/2376/115422
PMID: 11785931
Abstract
Synthesis of callose (β-1,3-glucan) in plants has been a topic of much debate over the past several decades. Callose synthase could not be purified to homogeneity and most partially purified cellulose synthase preparations yielded β-1,3-glucan in vitro, leading to the interpretation that cellulose synthase might be able to synthesize callose. While a rapid progress has been made on the genes involved in cellulose synthesis in the past five years, identification of genes for callose synthases has proven difficult because cognate genes had not been identified in other organisms. An Arabidopsis gene encoding a putative cell plate-specific callose synthase catalytic subunit (CalS1) was recently cloned. CalS1 shares high sequence homology with the well-characterized yeast β-1,3-glucan synthase and transgenic plant cells over-expressing CalS1 display higher callose synthase activity and accumulate more callose. The callose synthase complex exists in at least two distinct forms in different tissues and interacts with phragmoplastin, UDP-glucose transferase, Rop1 and, possibly, annexin. There are 12 CalS isozymes in Arabidopsis, and each may be tissue-specific and/or regulated under different physiological conditions responding to biotic and abiotic stresses.
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Details
- Title
- Plant callose synthase complexes
- Creators
- Desh Verma - Department of Molecular Genetics and Plant Biotechnology Center Ohio State University 1060 Carmack Road Columbus OH 43210 USAZonglie Hong - Department of Molecular Genetics and Plant Biotechnology Center Ohio State University 1060 Carmack Road Columbus OH 43210 USA
- Publication Details
- Plant molecular biology, Vol.47(6), pp.693-701
- Academic Unit
- Center for Reproductive Biology
- Publisher
- Kluwer Academic Publishers; Dordrecht
- Identifiers
- 99900547740001842
- Language
- English
- Resource Type
- Journal article