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


     

Plant Physiology 69:1414-1417 (1982)
© 1982 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 Hurkman, W. J.
Right arrow Articles by Beevers, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hurkman, W. J.
Right arrow Articles by Beevers, L.
Agricola
Right arrow Articles by Hurkman, W. J.
Right arrow Articles by Beevers, L.
Articles

Sequestration of Pea Reserve Proteins by Rough Microsomes 1

William J. Hurkman and Leonard Beevers

Department of Botany and Microbiology, University of Oklahoma, Norman, Oklahoma 73019

Free polysomes, polysomes released from membranes, and rough microsomal vesicles isolated from developing cotyledons of Pisum sativum L. cv. Burpeeana were used to direct cell-free protein synthesis in a wheat germ system. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that the polypeptide products had molecular weights ranging from 12,000 to 74,000. Some of the polypeptides migrated during electrophoresis with the same mobility as polypeptides present in legumin and vicilin preparations. By the use of rabbit antibodies raised against pea reserve proteins it was established that polysomes released from membranes and rough microsomes directed the synthesis of polypeptides that were related to reserve proteins whereas free polysomes did not.

Centrifugation studies indicated that the majority of the radioactivity incorporated by rough microsomes was specifically associated with the microsomes. The incorporated radioactivity of sedimented microsomes was not released by treatment with KCl and was resistant to proteolysis unless detergent was present. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the sequestered translation products were related to pea reserve proteins. It is concluded that the reserve proteins of pea cotyledons are synthesized exclusively by membrane-bound polysomes and that they are sequestered within the rough endoplasmic reticulum.

1 Supported by National Science Foundation grant PCM 7728273.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1982 by the American Society of Plant Biologists