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


     


This Article
Right arrow Full Text
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 Web of Science
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 Web of Science (26)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rotte, C.
Right arrow Articles by Leustek, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rotte, C.
Right arrow Articles by Leustek, T.
Agricola
Right arrow Articles by Rotte, C.
Right arrow Articles by Leustek, T.

Plant Physiol, October 2000, Vol. 124, pp. 715-724

Differential Subcellular Localization and Expression of ATP Sulfurylase and 5'-Adenylylsulfate Reductase during Ontogenesis of Arabidopsis Leaves Indicates That Cytosolic and Plastid Forms of ATP Sulfurylase May Have Specialized Functions1

Carmen Rotte2 and Thomas Leustek*

Biotechnology Center for Agriculture and the Environment, Rutgers University, New Brunswick, New Jersey 08901-8520

ATP sulfurylase and 5'-adenylylsulfate (APS) reductase catalyze two reactions in the sulfate assimilation pathway. Cell fractionation of Arabidopsis leaves revealed that ATP sulfurylase isoenzymes exist in the chloroplast and the cytosol, whereas APS reductase is localized exclusively in chloroplasts. During development of Arabidopsis plants the total activity of ATP sulfurylase and APS reductase declines by 3-fold in leaves. The decline in APS reductase can be attributed to a reduction of enzyme during aging of individual leaves, the highest activity occurring in the youngest leaves and the lowest in fully expanded leaves. By contrast, total ATP sulfurylase activity declines proportionally in all the leaves. The distinct behavior of ATP sulfurylase can be attributed to reciprocal expression of the chloroplast and cytosolic isoenzymes. The chloroplast form, representing the more abundant isoenzyme, declines in parallel with APS reductase during aging; however, the cytosolic form increases over the same period. In total, the results suggest that cytosolic ATP sulfurylase plays a specialized function that is probably unrelated to sulfate reduction. A plausible function could be in generating APS for sulfation reactions.


1 This work was supported by the National Science Foundation (grant nos. IBN-9601146 and IBN-9817594) and by the Studienstiftung des deutschen Volkes (to C.R.). The work was carried out in part as a Diplomarbeit Thesis from the Carl von Ossietzky Universität Oldenburg, Germany.

2 Present address: Institut fuer Botanik III, Heinrich-Heine Universitaet Duesseldorf, Universitaetsstrasse 1, 40225 Duesseldorf, Germany.

* Corresponding author; e-mail leustek{at}aesop.rutgers.edu; fax 732-932-0312.

© 2000 American Society of Plant Physiologists



This article has been cited by other articles:


Home page
Plant CellHome page
S. G. Mugford, N. Yoshimoto, M. Reichelt, M. Wirtz, L. Hill, S. T. Mugford, Y. Nakazato, M. Noji, H. Takahashi, R. Kramell, et al.
Disruption of Adenosine-5'-Phosphosulfate Kinase in Arabidopsis Reduces Levels of Sulfated Secondary Metabolites
PLANT CELL, March 1, 2009; 21(3): 910 - 927.
[Abstract] [Full Text] [PDF]


Home page
ANN BOT (LOND)Home page
S. KOPRIVA
Regulation of Sulfate Assimilation in Arabidopsis and Beyond
Ann. Bot., April 1, 2006; 97(4): 479 - 495.
[Abstract] [Full Text] [PDF]


Home page
Genome ResHome page
A. Adai, C. Johnson, S. Mlotshwa, S. Archer-Evans, V. Manocha, V. Vance, and V. Sundaresan
Computational prediction of miRNAs in Arabidopsis thaliana
Genome Res., January 1, 2005; 15(1): 78 - 91.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
K. Saito
Sulfur Assimilatory Metabolism. The Long and Smelling Road
Plant Physiology, September 1, 2004; 136(1): 2443 - 2450.
[Full Text] [PDF]


Home page
J Exp BotHome page
M. Klein and J. Papenbrock
The multi-protein family of Arabidopsis sulphotransferases and their relatives in other plant species
J. Exp. Bot., August 1, 2004; 55(404): 1809 - 1820.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
I. J. Pickering, C. Wright, B. Bubner, D. Ellis, M. W. Persans, E. Y. Yu, G. N. George, R. C. Prince, and D. E. Salt
Chemical Form and Distribution of Selenium and Sulfur in the Selenium Hyperaccumulator Astragalus bisulcatus
Plant Physiology, March 1, 2003; 131(3): 1460 - 1467.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
C. G. Ravina, C.-I. Chang, G. P. Tsakraklides, J. P. McDermott, J. M. Vega, T. Leustek, C. Gotor, and J. P. Davies
The sac Mutants of Chlamydomonas reinhardtii Reveal Transcriptional and Posttranscriptional Control of Cysteine Biosynthesis
Plant Physiology, December 1, 2002; 130(4): 2076 - 2084.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
B. L. Fatland, J. Ke, M. D. Anderson, W. I. Mentzen, L. W. Cui, C. C. Allred, J. L. Johnston, B. J. Nikolau, and E. S. Wurtele
Molecular Characterization of a Heteromeric ATP-Citrate Lyase That Generates Cytosolic Acetyl-Coenzyme A in Arabidopsis
Plant Physiology, October 1, 2002; 130(2): 740 - 756.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
A. Koprivova, M. Melzer, P. von Ballmoos, T. Mandel, C. Brunold, and S. Kopriva
Assimilatory Sulfate Reduction in C3, C3-C4, and C4 Species of Flaveria
Plant Physiology, October 1, 2001; 127(2): 543 - 550.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2000 by the American Society of Plant Biologists