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Heterogeneous distribution of pyruvate dehydrogenase in the matrix of mitochondria. | LitMetric

Heterogeneous distribution of pyruvate dehydrogenase in the matrix of mitochondria.

Mitochondrion

Department of Biology and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.

Published: February 2002

AI Article Synopsis

  • - A fusion protein combining GFP and E1alpha from the pyruvate dehydrogenase (PDH) complex was developed and successfully formed functional PDH complexes, verified through immunoprecipitation and activity assays.
  • - The GFP-E1alpha chimera is specifically expressed in mitochondria, showcasing two distinct fluorescence patterns: bright localized spots indicating assembled PDH complexes and uniform dim fluorescence representing unassembled proteins.
  • - The research highlights a non-uniform distribution of PDH complexes within the mitochondrial matrix, which persists over time and likely indicates the structural and metabolic compartmentalization of mitochondria in both normal and reduced PDH levels.

Article Abstract

A fusion protein between GFP and the E1alpha subunit of the pyruvate dehydrogenase (PDH) complex was created and shown to assemble into functional PDH complexes using immunoprecipitation and activity assays. The expression of this GFP-E1alpha chimera is specific to mitochondria and results in two different fluorescence patterns. These patterns have been distinguished by immunolabeling experiments using monoclonal antibodies against PDH subunits and GFP. The bright, localized fluorescent spots represent the assembled form of the GFP-E1alpha in PDH complexes. The uniform, dim fluorescence is given by the unassembled chimera free to diffuse throughout the mitochondrial reticulum. This study reveals a discrete, heterogeneous distribution of PDH complexes in the matrix of mitochondria, both in cells with normal and reduced levels of PDH. The uneven arrangement of PDH complexes is maintained over time and most likely reflects the structural and metabolic compartmentalization of mitochondria.

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Source
http://dx.doi.org/10.1016/s1567-7249(01)00033-2DOI Listing

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