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


     

This Article
Right arrow Full Text
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 ISI 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 HighWire
Right arrow Citing Articles via ISI Web of Science (10)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Stuger, R.
Right arrow Articles by Forreiter, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stuger, R.
Right arrow Articles by Forreiter, C.
Agricola
Right arrow Articles by Stuger, R.
Right arrow Articles by Forreiter, C.

Messenger RNA-Binding Properties of Nonpolysomal Ribonucleoproteins from Heat-Stressed Tomato Cells1

Rogier Stuger2, Sigrid Ranostaj, Tilo Materna3, and Christoph Forreiter*

Department of Molecular Cell Biology, Goethe University, Marie Curie Strasse 9, 60439 Frankfurt am Main, Germany

Most cells experiencing heat stress reprogram their translational machinery to favor the synthesis of heat-stress proteins. Translation of other transcripts is almost completely repressed, but most untranslated messengers are not degraded. In contrast to yeast, Drosophila melanogaster, and HeLa cells, plant cells store repressed messengers in cytoplasmic nonpolysomal ribonucleoproteins (RNPs). To follow the fate of untranslated transcripts, we studied protein composition, mRNA content, and RNA-binding properties of nonpolysomal RNPs from heat-stressed tomato (Lycopersicon peruvianum) cells. Contrary to the selective interaction in vivo, RNPs isolated from tomato cells bound both stress-induced and repressed messengers, suggesting that the selection mechanism resides elsewhere. This binding was independent of a cap or a poly(A) tail. The possible role of proteasomes and heat-stress granules (HSGs) in mRNA storage is a topic of debate. We found in vitro messenger-RNA-binding activity in messenger RNP fractions free of C2-subunit-containing proteasomes and HSGs. In addition, mRNAs introduced into tobacco (Nicotiana plumbaginifolia) protoplasts were found in the cytoplasm but were not associated with HSGs.

1   This work was funded by the Deutsche Forschungsgemeinschaft (grant no. No 249/1).
2   Present address: Department of Molecular Cell Physiology, Free University, de Boelelaan 1087, 1081 HV Amsterdam, The Netherlands.
3   Present address: Genetics Unit, Novartis Forschungsinstitut, Brunnerstrasse 59, 1235 Wien, Austria.
*   Corresponding author; e-mail forreiter{at}cellbiology.unifrankfurt.de; fax 49-69-798-29286.

Plant Physiol. (1999) 120: 23-32
Copyright Clearance Center:   0032-0889/99/120//10
© 1999 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
J. Ludwig-Müller, P. Krishna, and C. Forreiter
A Glucosinolate Mutant of Arabidopsis Is Thermosensitive and Defective in Cytosolic Hsp90 Expression after Heat Stress
Plant Physiology, July 1, 2000; 123(3): 949 - 958.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1999 by the American Society of Plant Biologists