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


     

Plant Physiology 82:760-764 (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 CrossRef
Right arrow Citing Articles via Web of Science (42)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mayfield, S. P.
Right arrow Articles by Taylor, W. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mayfield, S. P.
Right arrow Articles by Taylor, W. C.
Agricola
Right arrow Articles by Mayfield, S. P.
Right arrow Articles by Taylor, W. C.
Articles

The Fate of Chloroplast Proteins during Photooxidation in Carotenoid-Deficient Maize Leaves 1

Stephen P. Mayfield2, Timothy Nelson3 and William C. Taylor

Department of Genetics, University of California, Berkeley, California 94720

Maize seedlings, treated with the herbicide norflurazon to produce a deficiency in carotenoid pigments, were grown in low-fluence-rate light. Under these conditions, which induced chlorophyll biosynthesis while minimizing photooxidation, carotenoid-deficient seedlings showed identical patterns of chloroplast protein accumulation compared with normal seedlings. Carotenoid pigments thus play no direct role in regulating the accumulation of chloroplast proteins. When shifted to high-fluence-rate light, chlorophyll was rapidly photooxidized in carotenoid-deficient seedlings. Chloroplast proteins showed varying degrees of sensitivity to photooxidation. The P-700 apoprotein of photosystem I was rapidly degraded. Most stromal and thylakoid proteins either decreased progressively in photooxidative conditions or appeared to be unaffected. The relative quantity of the light-harvesting chlorophyll a/b-binding protein of photosystem II increased significantly in the first few hours of high-fluence-rate light. It then appeared to be only minimally affected 18 hours after complete photooxidation of chlorophyll.

2 Present address: Department de Biologie Moleculaire, Sciences II, Universite de Geneve, 30, quai Ernest-Ansermet, CH-1211 Geneve 4, Switzerland.

3 Present address: Department of Biology, Yale University, P.O. Box 6666, New Haven, CT 06511.

1 Supported by grants from the Competitive Research Grants Office of the United States Department of Agriculture to W. T.






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