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Protein Science, Vol 9, Issue 7 1334-1339, Copyright © 2000 by The Protein Society

The dihydrolipoyl acyltransferase (BCE2) subunit of the plant branched- chain alpha-ketoacid dehydrogenase complex forms a 24-mer core with octagonal symmetry [In Process Citation]

BP Mooney, MT Henzl, JA Miernyk and DD Randall
Biochemistry Department, University of Missouri, Columbia 65211, USA.

Little is known of the plant branched-chain alpha-ketoacid dehydrogenase complex. We have undertaken a detailed study of the structure of the dihydrolipoyl acyltransferase (BCE2) subunit that forms the core of the complex, to which two other enzymes attach. Mature Arabidopsis thaliana BCE2 was expressed in Escherichia coli. The soluble recombinant protein was purified using a Superose 6 size- exclusion column to >90% homogeneity and was catalytically active. The recombinant protein formed a stable complex with a native molecular mass of 0.95 MDa and an S coefficient of 19.4, consistent with formation of a 24-mer. Negative-staining transmission electron microscopy of the recombinant protein confirmed that BCE2 forms a core with octagonal symmetry. Despite divergence of mammalian and plant BCE2s, there is clearly conservation of structure that is independent of primary sequence.
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This article has been cited by other articles:


Home page
 Plant Physiol.Home page
N. L. Taylor, J. L. Heazlewood, D. A. Day, and A. H. Millar
Lipoic Acid-Dependent Oxidative Catabolism of {alpha}-Keto Acids in Mitochondria Provides Evidence for Branched-Chain Amino Acid Catabolism in Arabidopsis
Plant Physiology, February 1, 2004; 134(2): 838 - 848.
[Abstract] [Full Text] [PDF]


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