Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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 CrossRef
Right arrow Citing Articles via ISI Web of Science (17)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hatzack, F.
Right arrow Articles by Binder, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hatzack, F.
Right arrow Articles by Binder, S.
Agricola
Right arrow Articles by Hatzack, F.
Right arrow Articles by Binder, S.

Characterization of DNA-Binding Proteins from Pea Mitochondria1

Frank Hatzack2, Saskia Dombrowski, Axel Brennicke, and Stefan Binder*

Allgemeine Botanik, Universität Ulm, Albert-Einstein-Allee 11, D-89069 Ulm, Germany

We studied transcription initiation in the mitochondria of higher plants, with particular respect to promoter structures. Conserved elements of these promoters have been successfully identified by in vitro transcription systems in different species, whereas the involved protein components are still unknown. Proteins binding to double-stranded oligonucleotides representing different parts of the pea (Pisum sativum) mitochondrial atp9 were analyzed by denaturation-renaturation chromatography and mobility-shift experiments. Two DNA-protein complexes were detected, which appeared to be sequence specific in competition experiments. Purification by hydroxyapatite, phosphocellulose, and reversed-phase high-pressure liquid chromatography separated two polypeptides with apparent molecular masses of 32 and 44 kD. Both proteins bound to conserved structures of the pea atp9 and the heterologous Oenothera berteriana atp1 promoters and to sequences just upstream. Possible functions of these proteins in mitochondrial promoter recognition are discussed.


1   This work was supported by the Deutsche Forschungsgemeinschaft, a Landesforschungsschwerpunkt Baden-Württemberg, the Human Frontiers Science Program, and the Fonds der Chemischen Industrie.
2   Present address: Plant Genetics, Environmental Sciences and Technology Department, Risø National Laboratory, DK-4000 Roskilde, Denmark.
*   Corresponding author; e-mail stefan.binder{at}biologie.uni-ulm.de; fax 49-731-502-2626.

Plant Physiol. (1998) 116: 519-527
Copyright Clearance Center:   0032-0889/98/116/0519/09
© 1998 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
Mol. Cell. Biol.Home page
T. M. Ikeda and M. W. Gray
Characterization of a DNA-Binding Protein Implicated in Transcription in Wheat Mitochondria
Mol. Cell. Biol., December 1, 1999; 19(12): 8113 - 8122.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Dombrowski, M. Hoffmann, C. Guha, and S. Binder
Continuous Primary Sequence Requirements in the 18-Nucleotide Promoter of Dicot Plant Mitochondria
J. Biol. Chem., April 9, 1999; 274(15): 10094 - 10099.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
S. Mackenzie and L. McIntosh
Higher Plant Mitochondria
PLANT CELL, April 1, 1999; 11(4): 571 - 586.
[Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1998 by the American Society of Plant Biologists