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


     


Plant Physiology 44:912-922 (1969)
© 1969 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 CrossRef
Right arrow Citing Articles via Web of Science (90)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zucker, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zucker, M.
Agricola
Right arrow Articles by Zucker, M.
Articles

Induction of Phenylalanine Ammonia-lyase in Xanthium Leaf Disks. Photosynthetic Requirement and Effect of Daylength 1

Milton Zucker

a Department of Plant Pathology and Botany, The Connecticut Agricultural Experiment Station, New Haven, Connecticut 06504

A cycloheximide-sensitive increase in the activity of phenylalanine ammonia-lyase (EC 4.3.1.5) occurs in Xanthium leaf disks exposed to light. Radioactive ammonia-lyase has been isolated by means of sucrose density gradient centrifugation and starch gel electrophoresis from disks fed L-isoleucine-U-14C or L-arginine-U-14C. The incorporation of radioactive amino acids into phenylalanine ammonia-lyase together with the inhibitory effects of cycloheximide indicate that the observed increase in enzyme activity involves the induction of lyase synthesis.

The light-dependent synthesis of the ammonia-lyase is completely inhibited by 50 µM 3-(4-chlorophenyl)-1,1-dimethylurea (CMU) indicating that photosynthesis is involved. Only a trace quantity of some photosynthetic product must be needed because half light saturation occurs at very low intensity (ca. 30 ft-c). Exogenous carbohydrate is also required for continuing enzyme synthesis over a 72 hr period. But carbohydrate does not replace the photosynthetic requirement in darkness.

Enzyme formed in light disappears rapidly from disks placed in the dark. The decay of ammonia-lyase activity follows first order kinetics. The half-life of the lyase ranged from 6 to 15 hr in leaf material used. Cyoloheximide inhibits the decay of lyase activity. Thus the maintenance of turnover in Xanthium leaf disks requires de novo synthesis of protein. That turnover, i.e., degradation as well as synthesis of lyase protein occurs is suggested by the apparent loss of radioactive ammonia-lyase from leaf disks placed in darkness. Light-induced synthesis coupled with rapid turnover can produce a diurnal fluctuation of ammonia-lyase activity in Xanthium leaf disks. Alternating periods of enzyme synthesis and degradation were observed in disks exposed to 24 hr cycles of light and dark. The average level of enzyme activity maintained in the tissue was directly related to the length of the light period. Induction of lyase synthesis was also observed in excised leaves and to a lesser extent in leaves of whole plants.


1 Supported in part by grant GB 6702 from NSF. A preliminary report of this work has appeared (38).







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1969 by the American Society of Plant Biologists