A novel regulatory mechanism based upon a dynamic core structure for the mitochondrial pyruvate dehydrogenase complex?

Mitochondrion. 2014 Nov:19 Pt B:144-53. doi: 10.1016/j.mito.2014.05.003. Epub 2014 May 17.

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.

Keywords: BiFC; Protein interaction; Regulation; Structure; Transmission Electron Microscopy.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / chemistry
  • Arabidopsis / enzymology*
  • Arabidopsis / metabolism
  • Dihydrolipoyllysine-Residue Acetyltransferase / chemistry
  • Dihydrolipoyllysine-Residue Acetyltransferase / metabolism*
  • Gene Expression Regulation, Enzymologic*
  • Gene Expression Regulation, Plant*
  • Macromolecular Substances / ultrastructure
  • Microscopy, Electron, Transmission
  • Mitochondrial Proteins / metabolism*
  • Protein Multimerization
  • Pyruvate Dehydrogenase Complex / chemistry
  • Pyruvate Dehydrogenase Complex / metabolism*

Substances

  • Macromolecular Substances
  • Mitochondrial Proteins
  • Pyruvate Dehydrogenase Complex
  • Dihydrolipoyllysine-Residue Acetyltransferase