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A novel regulatory mechanism based upon a dynamic core structure for the mitochondrial pyruvate dehydrogenase complex?
- Source :
-
Mitochondrion [Mitochondrion] 2014 Nov; Vol. 19 Pt B, pp. 144-53. Date of Electronic Publication: 2014 May 17. - Publication Year :
- 2014
-
Abstract
- The Arabidopsis thaliana genome includes three genes for mitochondrial dihydrolipoamide acetyltransferase, the E2-component of the mitochondrial pyruvate dehydrogenase complex (PDC). Two genes encode E2-proteins with a single lipoyl domain, while the third has a two-lipoyl domain structure. Transcripts for each E2 protein were expressed in all plant organs. Each recombinant AtmtE2 can individually form an icosahedral PDC core structure, and results from bimolecular fluorescence complementation assays are consistent with formation of hetero-core structures from all permutations of the AtmtE2 proteins. We propose a unique regulatory mechanism involving dynamic formation of hetero-core complexes that include both mono- and di-lipoyl forms of AtmtE2.<br /> (Copyright © 2014 Elsevier B.V. and Mitochondria Research Society. All rights reserved.)
- Subjects :
- Arabidopsis chemistry
Arabidopsis metabolism
Dihydrolipoyllysine-Residue Acetyltransferase chemistry
Macromolecular Substances ultrastructure
Microscopy, Electron, Transmission
Protein Multimerization
Pyruvate Dehydrogenase Complex chemistry
Arabidopsis enzymology
Dihydrolipoyllysine-Residue Acetyltransferase metabolism
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
Mitochondrial Proteins metabolism
Pyruvate Dehydrogenase Complex metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1872-8278
- Volume :
- 19 Pt B
- Database :
- MEDLINE
- Journal :
- Mitochondrion
- Publication Type :
- Academic Journal
- Accession number :
- 24846799
- Full Text :
- https://doi.org/10.1016/j.mito.2014.05.003