ORIGINAL RESEARCH

Two HMG domains of yeast mitochondrial protein Abf2p have different affinity to DNA

Kurashenko AV1, Samoilova EO1, Balaeva MV1, Chicherin IV1, Petrov DYu2, Kamenski P1, Levitskii SA1
About authors

1 Department of Molecular Biology, Faculty of Biology,
Lomonosov Moscow State University, Moscow, Russia

2 Department of General Surgery, Faculty of Fundamental Medicine,
Lomonosov Moscow State University, Moscow, Russia

Correspondence should be addressed: Peter Kamenski
Leninskie gory, d. 1, str. 12, Moscow, Russia, 119991; moc.liamg@iksnemak.rtoip

About paper

Funding: this study was supported by the Russian Foundation for Basic Research (project no. 14-04-31554 mol_a).

Received: 2015-09-29 Accepted: 2015-12-09 Published online: 2017-01-05
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Maintaining mitochondrial genome integrity is essential for the viability of the whole organism. Mitochondrial genome mutations lead to muscular dystrophies, neurodegenerative diseases, and are associated with aging. In this work a baker’s yeast (Saccharomyces cerevisiae) mitochondria model was used to investigate DNA-binding abilities of different domains of a mitochondrial Abf2p protein which participates in homologous recombination and reparation. A weak non-specific HMG1 binding to linear DNA and a specific HMG1 binding to a branched DNA with a dissociation constant of 510 nM have been discovered. The HMG2 domain itself does not bind to any DNA and either has other functions or demonstrates its DNA-binding activity in a full-length protein only.

Keywords: mitochondria, mitochondrial genome, Abf2p, recombination

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