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

被引:8
作者
Bakkaiova, Jana [1 ,2 ]
Marini, Victoria [3 ,4 ]
Willcox, Smaranda [5 ]
Nosek, Jozef [1 ,2 ]
Griffith, Jack D. [5 ]
Krejci, Lumir [3 ,4 ,6 ]
Tomaska, Lubomir [1 ,2 ]
机构
[1] Comenius Univ, Fac Nat Sci, Dept Genet, Ilkovicova 6, Bratislava 84215, Slovakia
[2] Comenius Univ, Fac Nat Sci, Dept Biochem, Ilkovicova 6, Bratislava 84215, Slovakia
[3] Masaryk Univ, Dept Biol, Kamenice 5-A7, Brno 62500, Czech Republic
[4] St Annes Univ Hosp Brno, Int Clin Res Ctr, Brno 60200, Czech Republic
[5] Univ N Carolina, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA
[6] Masaryk Univ, Natl Ctr Biomol Res, Kamenice 5-A7, Brno 62500, Czech Republic
基金
美国国家卫生研究院;
关键词
DNA-binding protein; DNA compaction; HMG-box containing protein; Holliday junction; mitochondrial DNA (mtDNA); mitochondrial nucleoid; MOBILITY GROUP PROTEIN; FIELD GEL-ELECTROPHORESIS; TRANSCRIPTION FACTOR-I; CANDIDA-PARAPSILOSIS; SACCHAROMYCES-CEREVISIAE; TELOMERE MAINTENANCE; STRUCTURAL-ANALYSIS; PACKAGING PROTEIN; MOVING-PICTURES; BOX PROTEIN;
D O I
10.1042/BSR20150275
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Yeast mtDNA is compacted into nucleoprotein structures called mitochondrial nucleoids (mt-nucleoids). The principal mediators of nucleoid formation are mitochondrial high-mobility group (HMG)-box containing (mtHMG) proteins. Although these proteins are some of the fastest evolving components of mt-nucleoids, 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 the present 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 dsDNA. 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 (HJ) and replication forks (RF). 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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页数:13
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