A β-like DNA polymerase from the mitochondrion of the trypanosomatid Crithidia fasciculata

Al F. Torri, Thomas A. Kunkel, Paul T. Englund

Research output: Contribution to journalArticle

Abstract

The mitochondrial DNA in Crithidia fasciculata, a trypanosomatid parasite, is known as kinetoplast DNA. Kinetoplast DNA has a very unusual structure, consisting of several thousand minicircles and a few dozen maxicircles, all topologically interlocked into a giant network. There is one network within each cell's single mitochondrion. We previously purified a 43-kDa DNA polymerase from C. fasciculata mitochondria (Torri, A. F., and Englund, P. T. (1992) J. Biol. Chem. 267, 4786-4792). This enzyme has properties very different from those of a DNA polymerase γ, the conventional mitochondrial polymerase. In addition to its small size, it is nonprocessive, has no detectable exonuclease activity, and has very low fidelity. In all of these respects, the polymerase resembles a DNA polymerase β, a gap-filling enzyme thought to function in DNA repair in the nucleus of other eukaryotes. We speculate that this enzyme may have been specially imported into the C. fasciculata mitochondrion to repair the many gaps found in minicircles following their replication. This is the first example of a β-like polymerase from the mitochondrion of any eukaryote.

Original languageEnglish (US)
Pages (from-to)8165-8171
Number of pages7
JournalJournal of Biological Chemistry
Volume269
Issue number11
StatePublished - Mar 18 1994

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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