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


     


Plant Physiology 82:390-395 (1986)
© 1986 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 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 (34)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Snapp, S. S.
Right arrow Articles by Vance, C. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Snapp, S. S.
Right arrow Articles by Vance, C. P.
Agricola
Right arrow Articles by Snapp, S. S.
Right arrow Articles by Vance, C. P.
Articles

Asparagine Biosynthesis in Alfalfa (Medicago sativa L.) Root Nodules 1

Sieglinde S. Snapp and Carroll P. Vance

The Department of Agronomy and Plant Genetics, University of Minnesota, St. Paul, Minnesota 55108, The United States Department of Agriculture, Agricultural Research Service, University of Minnesota, St. Paul, Minnesota 55108

Rapid direct conversion of exogenously supplied [14C]aspartate to [14C] asparagine and to tricarboxylic cycle acids was observed in alfalfa (Medicago sativa L.) nodules. Aspartate aminotransferase activity readily converted carbon from exogenously applied [14C]aspartate into the tricarboxylic acid cycle with subsequent conversion to the organic acids malate, succinate, and fumarate. Aminooxyacetate, an inhibitor of aminotransferase activity, reduced the flow of carbon from [14C]aspartate into tricarboxylic cycle acids and decreased 14CO2 evolution by 99%. Concurrently, maximum conversion of aspartate to asparagine was observed in aminooxyacetate treated nodules (30 nanomoles asparagine per gram fresh weight per hour. Metabolism of [14C]aspartate and distribution of nodulefixed 14CO2 suggest that two pools of aspartate occur in alfalfa nodules: (a) one involved in asparagine biosynthesis, and (b) another supplying a malate/aspartate shuttle. Conversion of [14C]aspartate to [14C]asparagine was not inhibited by methionine sulfoximine, a glutamine synthetase inhibitor, or azaserine, a glutmate synthetase, inhibitor. The data did not indicate that asparagine biosynthesis in alfalfa nodules has an absolute requirement for glutamine. Radioactivity in the xylem sap, derived from nodule 14CO2 fixation, was markedly decreased by treating nodulated roots with aminooxyacetate, methionine sulfoximine, and azaserine. Inhibitors decreased the [14C]aspartate and [14]asparagine content of xylem sap by greater than 80% and reduced the total amino nitrogen content of xylem sap (including nonradiolabeled amino acids) by 50 to 80%. Asparagine biosynthesis in alfalfa nodules and transport in xylem sap are dependent upon continued aminotransferase activity and an uninterrupted assimilation of ammonia via the glutamine synthetase/glutamate synthase pathway. Continued assimilation of ammonia apparently appears crucial to continued root nodule CO2 fixation in alfalfa.


1 Joint contribution from the Minnesota Agriculture Experiment Station (Paper No. 14,841, Scientific Journal Series) and United States Department of Agriculture-Agricultural Research Service.




This article has been cited by other articles:


Home page
Plant Physiol.Home page
A. M. Scharff, H. Egsgaard, P. E. Hansen, and L. Rosendahl
Exploring Symbiotic Nitrogen Fixation and Assimilation in Pea Root Nodules by in Vivo 15N Nuclear Magnetic Resonance Spectroscopy and Liquid Chromatography-Mass Spectrometry
Plant Physiology, January 1, 2003; 131(1): 367 - 378.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
G. B. Trepp, D. W. Plank, J. Stephen Gantt, and C. P. Vance
NADH-Glutamate Synthase in Alfalfa Root Nodules. Immunocytochemical Localization
Plant Physiology, March 1, 1999; 119(3): 829 - 838.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1986 by the American Society of Plant Biologists