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

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Publikace nespadá pod Filozofickou fakultu, ale pod Lékařskou fakultu. Oficiální stránka publikace je na webu muni.cz.
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BAKKAIOVA Jana MARINI PALOMEQUE María Victoria WILLCOX Smaranda NOSEK Jozef GRIFFITH Jack D. KREJČÍ Lumír TOMASKA Lubomir

Rok publikování 2016
Druh Článek v odborném periodiku
Časopis / Zdroj Bioscience Reports
Fakulta / Pracoviště MU

Lékařská fakulta

Citace
Doi http://dx.doi.org/10.1042/BSR20150275
Obor Genetika a molekulární biologie
Klíčová slova DNA binding protein; DNA compaction; HMG-box containing protein; mitochondrial DNA (mtDNA); Holliday junction; mitochondrial nucleoid
Popis Yeast mitochondrial DNA (mtDNA) is compacted into nucleoprotein structures called mitochondrial nucleoids (mt-nucleoids). The principal mediators of nucleoid formation are mitochondrial HMG-box containing (mtHMG) proteins. Although these proteins are some of the fastest evolving components of mtnucleoids, it is not known whether the divergence of mtHMG proteins on the level of their amino acid sequences is accompanied by diversification of their biochemical properties. In this study we performed a comparative biochemical analysis of yeast mtHMG proteins from Saccharomyces cerevisiae (ScAbf2p), Yarrowia lipolytica (YlMhb1p) and Candida parapsilosis (CpGcf1p). We found that all three proteins exhibit relatively weak binding to intact double-stranded (ds) DNA. In fact, ScAbf2p and YlMhb1p bind quantitatively to this substrate only at very high protein to DNA ratios and CpGcf1p shows only negligible binding to dsDNA. In contrast, the proteins exhibit much higher preference for recombination intermediates such as Holliday junctions and replication forks. Therefore, we hypothesize that the roles of the yeast mtHMG proteins in maintenance and compaction of mtDNA in vivo are in large part mediated by their binding to recombination/replication intermediates. We also speculate that the distinct biochemical properties of CpGcf1p may represent one of the prerequisites for frequent evolutionary tinkering with the form of the mitochondrial genome in the CTG-clade of hemiascomycetous yeast species.
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