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


     

Plant Physiology 75:516-520 (1984)
© 1984 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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Beudeker, R. F.
Right arrow Articles by Tabita, F. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Beudeker, R. F.
Right arrow Articles by Tabita, F. R.
Agricola
Right arrow Articles by Beudeker, R. F.
Right arrow Articles by Tabita, F. R.
Articles

Glycolate Metabolism Is Under Nitrogen Control in Chlorella1

Rob F. Beudeker2 and F. Robert Tabita

Center for Applied Microbiology, The University of Texas at Austin, Austin, Texas 78712-1095, Department of Microbiology, The University of Texas at Austin, Austin, Texas 78712-1095

The utilization of nitrate and ammonia as nitrogen sources had different effects on the metabolism of glycolate in Cholorella sorokiniana. During photolithotrophic growth with nitrate as nitrogen source, glycolate was metabolized via the glycine-serine pathway. Ammonia, produced as a result of glycolate metabolism, was reassimilated by glutamine synthetase. Two isoforms of this enzyme were present at different relative abundance in C. sorokiniana wild type and in a mutant with an increased capacity for the metabolism of glycolate (strain OR).

During photolithotrophic growth in the presence of ammonia as sole nitrogen source, several lines of evidence indicated that glycolate was metabolized to malate, pyruvate, tricarboxylic acid cycle intermediates and related amino acids in C. sorokiniana wild-type cells. Malate synthase was induced and glycine decarboxylase and serine-glyoxylate aminotransferase were repressed in cells grown with ammonia. An inverse correlation was observed between aminating NADPH-glutamate dehydrogenase and the in vivo glycine decarboxylation rate.

2 Present address: R. F. Beudeker, Gist-Brocades, Section FOG, 2600 MA Delft, The Netherlands.

1 Supported by Dow Chemical Company. A preliminary account of these investigations was presented at the Third International Symposium on Microbial Growth of C1 Compounds, held in Minneapolis from September 6-10, 1983.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1984 by the American Society of Plant Biologists