The mitochondrial DNA polymerase βfrom Crithidia fasciculata has 5′-deoxyribose phosphate (dRP) lyase activity but is deficient in the release of dRP

Tina T. Saxowsky, Yoshihiro Matsumoto, Paul T. Englund

Research output: Contribution to journalArticlepeer-review

Abstract

DNA polymerase β (pol β) has long been described as a nuclear enzyme involved in DNA repair. A pol β from the trypanosomatid parasite Crithidia fasciculata, however, is the first example of a mitochondrial enzyme of this type. The mammalian nuclear enzyme functions not only as a nucleotidyl transferase but also has a dRP lyase activity that cleaves 5′-deoxyribose phosphate (dRP) groups from DNA, thus contributing to two consecutive steps of the base excision repair pathway. We find that the mitochondrial pol β also has dRP lyase activity. Interestingly, the Km of this enzyme for a dRP-containing substrate is similar to that for the rat enzyme, but its kcat is very low. This difference is due to a deficiency of the mitochondrial enzyme in the release of dRP from the enzyme following its cleavage from the DNA.

Original languageEnglish (US)
Pages (from-to)37201-37206
Number of pages6
JournalJournal of Biological Chemistry
Volume277
Issue number40
DOIs
StatePublished - Oct 4 2002

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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