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


     

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 (21)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by D'Hondt, K.
Right arrow Articles by Krebbers, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by D'Hondt, K.
Right arrow Articles by Krebbers, E.
Agricola
Right arrow Articles by D'Hondt, K.
Right arrow Articles by Krebbers, E.

PLANT PHYSIOLOGY , Vol 102, Issue 2 425-433, Copyright © 1993 by American Society of Plant Biologists

CELL BIOLOGY AND SIGNAL TRANSDUCTION

Studies of the Role of the Propeptides of the Arabidopsis thaliana 2S Albumin

K. D'Hondt, J. Van Damme, C. Van Den Bossche, S. Leejeerajumnean, R. De Rycke, J. Derksen, J. Vandekerckhove and E. Krebbers
Plant Genetic Systems, Plateaustraat 22, B-9000 Gent, Belgium (K.D'H., J.V.D., E.K.)

To investigate the possible roles of the Arabidopsis thaliana 2S albumin propeptides with respect to sorting, processing, and stability of the protein in plant cells, five gene constructions deleting or modifying the propeptides were made based on one of the genes encoding the Arabidopsis 2S albumin. These constructions were introduced into tobacco (Nicotiana tabacum) plants. Using subcellular fractionation and immunocytochemistry on ripe seeds, it was demonstrated that none of the propeptides was necessary for the sorting of the protein. Detailed protein-chemical analysis of the mature gene products indicated that, for all of the modified 2S albumin precursors made, the proteins were stably folded and correctly processed. However, the latter is less efficient when the internal fragment between the small and the large subunit is missing or when this internal fragment is changed. In an attempt to establish a rapid assay system for modified 2S albumin precursors, yeast cells were transformed with the same gene constructs. It was demonstrated that the processing machinery in yeast cells differs from that in plants, and, in a perhaps related observation, differences in stability of a particular modified protein were observed.




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1993 by the American Society of Plant Biologists