Yeast mitochondrial HMG proteins: DNA-binding properties of the most evolutionarily divergent component of

Jana Bakkaiova1, Victoria Marini2, Smaranda Willcox3

  • 1Departments of Genetics and Biochemistry, Comenius University in Bratislava, Faculty of Natural Sciences, Mlynska dolina, Ilkovicova 6, 842 15 Bratislava, Slovak Republic.

Bioscience Reports
|December 10, 2015
PubMed

Insights

Yeast mitochondrial high-mobility group (HMG)-box containing (mtHMG) proteins bind weakly to dsDNA but prefer DNA recombination intermediates. This suggests their role in mitochondrial DNA maintenance involves these structures.

Area of Science:

  • Mitochondrial genetics
  • Molecular biology
  • Yeast genetics

Background:

  • Yeast mitochondrial DNA (mtDNA) is organized into nucleoprotein structures known as mitochondrial nucleoids (mt-nucleoids).
  • Mitochondrial high-mobility group (HMG)-box containing (mtHMG) proteins are key mediators of mt-nucleoid formation.
  • mtHMG proteins are among the fastest evolving components of mt-nucleoids, but their biochemical properties remain largely unexplored.

Purpose of the Study:

  • To investigate whether the amino acid sequence divergence of yeast mtHMG proteins is associated with diversification in their biochemical properties.
  • To compare the DNA-binding characteristics of mtHMG proteins from different yeast species.

Main Methods:

  • Comparative biochemical analysis of mtHMG proteins from Saccharomyces cerevisiae (ScAbf2p), Yarrowia lipolytica (YlMhb1p), and Candida parapsilosis (CpGcf1p).
  • Assessment of protein binding affinities to intact double-stranded DNA (dsDNA), Holliday junctions (HJ), and replication forks (RF).

Main Results:

  • All three analyzed mtHMG proteins exhibited weak binding to intact dsDNA.
  • ScAbf2p and YlMhb1p showed quantitative binding to dsDNA only at very high protein concentrations.
  • CpGcf1p demonstrated negligible binding to dsDNA.
  • In contrast, all three proteins displayed significantly higher preference for binding to DNA recombination intermediates like HJ and RF.

Conclusions:

  • Yeast mtHMG proteins likely play a crucial role in mtDNA maintenance and compaction in vivo through their preferential binding to recombination and replication intermediates.
  • The distinct biochemical properties of CpGcf1p may contribute to the evolutionary flexibility observed in the mitochondrial genome structure within the CTG-clade yeast species.

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