ORIGINAL RESEARCH
Two HMG domains of yeast mitochondrial protein Abf2p have different affinity to DNA
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
Funding: this study was supported by the Russian Foundation for Basic Research (project no. 14-04-31554 mol_a).
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