Plant Physiology Preview
Published on March 7, 2002; 10.1104/pp.010925
Received October 9, 2001
Returned for revision December 15, 2001
Accepted January 1, 2002
Guard Cell- and Phloem Idioblast-Specific Expression of
Thioglucoside Glucohydrolase 1 (Myrosinase) in
Arabidopsis
Harald Husebye , Supachitra Chadchawan , Per Winge , Ole P. Thangstad , and Atle M. Bones *
Department of Botany, Norwegian University of Science and Technology, N--7491 Trondheim, Norway (H.H., P.W., O.P.T., A.M.B.); and Department of Botany, Chulalongkorn University, Bangkok 10330, Thailand (S.C.)
* Corresponding author; email: atle.bones{at}chembio.ntnu.no.
Thioglucoside glucohydrolase 1 (TGG1) is one of two known functional myrosinase enzymes in Arabidopsis. The enzyme catalyzes the hydrolysis of glucosinolates into compounds that are toxic to various microbes and herbivores. Transgenic Arabidopsis plants carrying ß-glucuronidase and green fluorescent protein reporter genes fused to 0.5 or 2.5 kb of the TGG1 promoter region were used to study spatial promoter activity. Promoter activity was found to be highly specific and restricted to guard cells and distinct cells of the phloem. No promoter activity was detected in the root or seed. All guard cells show promoter activity. Positive phloem cells are distributed in a discontinuous pattern and occur more frequent in young tissues. Immunocytochemical localization of myrosinase in transverse and longitudinal sections of embedded material show that the TGG1 promoter activity reflects the position of the myrosinase enzyme. In the flower stalk, the myrosinase-containing phloem cells are located between phloem sieve elements and glucosinolate-rich S cells. Our results suggest a cellular separation of myrosinase enzyme and glucosinolate substrate, and that myrosinase is contained in distinct cells. We discuss the potential advantages of locating defense and communication systems to only a few specific cell types.
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