Plant Cell BGI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


First published online March 2, 2010; 10.1105/tpc.109.073726

The Plant Cell 22:797-810 (2010)
© 2010 American Society of Plant Biologists

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow PPT slides of all figures
Right arrow Supplemental Data
Right arrow All Versions of this Article:
22/3/797    most recent
tpc.109.073726v1
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
Google Scholar
Right arrow Articles by Klodmann, J.
Right arrow Articles by Braun, H. P.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Klodmann, J.
Right arrow Articles by Braun, H. P.
Agricola
Right arrow Articles by Klodmann, J.
Right arrow Articles by Braun, H. P.

RESEARCH ARTICLES

Internal Architecture of Mitochondrial Complex I from Arabidopsis thaliana

Jennifer Klodmanna, Stephanie Sunderhausa, Manfred Nimtzb, Lothar Jänschb and Hans-Peter Brauna,1

a Institute for Plant Genetics, Faculty of Natural Sciences, Leibniz Universität Hannover, D-30419 Hannover, Germany
b Proteome Research Group, Division of Cell and Immune Biology, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany

1 Address correspondence to braun{at}genetik.uni-hannover.de.

The NADH dehydrogenase complex (complex I) of the respiratory chain has unique features in plants. It is the main entrance site for electrons into the respiratory electron transfer chain, has a role in maintaining the redox balance of the entire plant cell and additionally comprises enzymatic side activities essential for other metabolic pathways. Here, we present a proteomic investigation to elucidate its internal structure. Arabidopsis thaliana complex I was purified by a gentle biochemical procedure that includes a cytochrome c–mediated depletion of other respiratory protein complexes. To examine its internal subunit arrangement, isolated complex I was dissected into subcomplexes. Controlled disassembly of the holo complex (1000 kD) by low-concentration SDS treatment produced 10 subcomplexes of 550, 450, 370, 270, 240, 210, 160, 140, 140, and 85 kD. Systematic analyses of subunit composition by mass spectrometry gave insights into subunit arrangement within complex I. Overall, Arabidopsis complex I includes at least 49 subunits, 17 of which are unique to plants. Subunits form subcomplexes analogous to the known functional modules of complex I from heterotrophic eukaryotes (the so-called N-, Q-, and P-modules), but also additional modules, most notably an 85-kD domain including {gamma}-type carbonic anhydrases. Based on topological information for many of its subunits, we present a model of the internal architecture of plant complex I.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications THE PLANT CELL PLANT PHYSIOLOGY
Copyright © 2010 by the American Society of Plant Biologists