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 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 HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Van den Broeck, D.
Right arrow Articles by Caplan, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Van den Broeck, D.
Right arrow Articles by Caplan, A.
Agricola
Right arrow Articles by Van den Broeck, D.
Right arrow Articles by Caplan, A.

PLANT PHYSIOLOGY , Vol 106, Issue 2 559-566, Copyright © 1994 by American Society of Plant Biologists

MOLECULAR BIOLOGY AND GENE REGULATION

A Group of Chromosomal Proteins Is Specifically Released by Spermine and Loses DNA-Binding Activity upon Phosphorylation

D. Van den Broeck, D. Van Der Straeten, M. Van Montagu and A. Caplan
Laboratorium voor Genetica, Universiteit Gent, B-9000 Gent, Belgium

Biologically relevant concentrations as low as 500 [mu]M spermine led to the specific release of chromatin-associated proteins from nuclei of rice (Oryza sativa) seedlings. Using a southwestern technique, it was shown that several of these proteins bind DNA. This affinity was lost upon in organello phosphorylation by an endogenous kinase. The effect of spermine was very specific. Spermidine was far less effective and putrescine was essentially ineffective in releasing these proteins. The most abundant spermine-released protein was shown to be homologous to the maize HMG1 protein. Our results suggest that spermine induces the release of spermine-released proteins by changing DNA conformation. Binding of these proteins might be sensitive to long-range changes in chromosome structure caused by torsional stress.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
Q. Yuan, M. J. Viar, R. M. Ray, and L. R. Johnson
Putrescine does not support the migration and growth of IEC-6 cells
Am J Physiol Gastrointest Liver Physiol, January 1, 2000; 278(1): G49 - G56.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1994 by the American Society of Plant Biologists