Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Plant Physiology 72:287-290 (1983)
© 1983 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jonsson, L. M. V.
Right arrow Articles by Schram, A. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jonsson, L. M. V.
Right arrow Articles by Schram, A. W.
Agricola
Right arrow Articles by Jonsson, L. M. V.
Right arrow Articles by Schram, A. W.
Articles

Subcellular Localization of Anthocyanin Methyltransferase in Flowers of Petunia hybrida

Lisbeth M. V. Jonsson, Wilma E. Donker-Koopman, Piet Uitslager and André W. Schram

Department of Plant Physiology, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands, Department of Genetics, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands

The subcellular localization of the enzyme anthocyanin-methyltransferase was studied in cells (protoplasts) obtained from the upper epidermis of petals of Petunia hybrida Hort. Vacuoles were isolated from protoplasts to ascertain the possible presence of the enzyme in these organelles. The recovery of methyltransferase activity in vacuole-enriched fractions equalled that of the cytosolic marker enzyme glucose-6-phosphate dehydrogenase. The relative activity of methyltransferase in the vacuole fraction was one tenth of that in the protoplast. Neither whole protoplasts nor isolated vacuoles contained inhibitors of methyltransferase activity. Examination of fractions obtained by differential centrifugation of a protoplast lysate showed that the major part of the methyltransferase activity was cytosolic. Activity found in a 130,000g pellet was due to nonspecific adhesion to membranes. The results indicate that terminal steps of anthocyanin biosynthesis take place in the cytosol. They do not lend support to the notion that the vacuole might be involved in (part of) this process.




This article has been cited by other articles:


Home page
 J Exp BotHome page
S. Conn, C. Curtin, A. Bezier, C. Franco, and W. Zhang
Purification, molecular cloning, and characterization of glutathione S-transferases (GSTs) from pigmented Vitis vinifera L. cell suspension cultures as putative anthocyanin transport proteins
J. Exp. Bot., October 1, 2008; 59(13): 3621 - 3634.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
W. Xu, H. Shioiri, M. Kojima, and M. Nozue
Primary Structure and Expression of a 24-kD Vacuolar Protein (VP24) Precursor in Anthocyanin-Producing Cells of Sweet Potato in Suspension Culture
Plant Physiology, January 1, 2001; 125(1): 447 - 455.
[Abstract] [Full Text]

Home page
 ScienceHome page
B. A. Snyder and R. L. Nicholson
Synthesis of Phytoalexins in Sorghum as a Site-Specific Response to Fungal Ingress
Science, June 29, 1990; 248(4963): 1637 - 1639.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1983 by the American Society of Plant Biologists