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Submitted on April 18, 2003
Pharmacological Sciences, University at Stony Brook, Stony Brook, NY 11794-8651
Corresponding Author: dan{at}pharm.sunysb.edu
Mitochondrial DNA (mtDNA) is not packaged in nucleosomal particles, but has been reported to associate with the mitochondrial inner membrane. Gentle lysis of Xenopus oocyte mitochondria with non-ionic detergent liberates a nucleoprotein complex containing mtDNA associated with a previously characterized DNA binding partner, mtTFA, as well as a series of inner membrane proteins identified by sequencing. More extensive detergent treatment stripped most of these proteins from the DNA leaving a limited number of proteins in a nucleoid core. Sequencing of the major proteins retained in association with mtDNA revealed the expected mtDNA binding proteins, mtTFA and mtSSB, as well as four proteins not previously reported to associate with mtDNA. These include adenine nucleotide translocator 1, the lipoyl-containing E2 subunits of pyruvate dehydrogenase and branched chain a-ketoacid dehydrogenase and prohibitin 2. The association of several of these proteins with mtTFA-containing mtDNA nucleoids was confirmed by immunoprecipitation.
Revised on September 26, 2003
Accepted on September 26, 2003
Protein components of mitochondrial DNA nucleoids in higher eukaryotes
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