| BAKKAIOVA, Jana, María Victoria MARINI PALOMEQUE, Smaranda WILLCOX, Jozef NOSEK, Jack D. GRIFFITH, Lumír KREJČÍ and Lubomir TOMASKA. Yeast mitochondrial HMG proteins: DNA-binding properties of the most evolutionarily divergent component of mitochondrial nucleoids. Bioscience Reports. London: Portland Press LTD, 2016, vol. 36, No 1, p. "nestránkováno", 13 pp. ISSN 0144-8463. Available from: https://dx.doi.org/10.1042/BSR20150275. |
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@article{1331439,
author = {Bakkaiova, Jana and Marini Palomeque, María Victoria and Willcox, Smaranda and Nosek, Jozef and Griffith, Jack D. and Krejčí, Lumír and Tomaska, Lubomir},
article_location = {London},
article_number = {1},
doi = {http://dx.doi.org/10.1042/BSR20150275},
keywords = {DNA binding protein; DNA compaction; HMG-box containing protein; mitochondrial DNA (mtDNA); Holliday junction; mitochondrial nucleoid},
language = {eng},
issn = {0144-8463},
journal = {Bioscience Reports},
title = {Yeast mitochondrial HMG proteins: DNA-binding properties of the most evolutionarily divergent component of mitochondrial nucleoids},
volume = {36},
year = {2016}
}
TY - JOUR
ID - 1331439
AU - Bakkaiova, Jana - Marini Palomeque, María Victoria - Willcox, Smaranda - Nosek, Jozef - Griffith, Jack D. - Krejčí, Lumír - Tomaska, Lubomir
PY - 2016
TI - Yeast mitochondrial HMG proteins: DNA-binding properties of the most evolutionarily divergent component of mitochondrial nucleoids
JF - Bioscience Reports
VL - 36
IS - 1
SP - "nestránkováno"
EP - "nestránkováno"
PB - Portland Press LTD
SN - 01448463
KW - DNA binding protein
KW - DNA compaction
KW - HMG-box containing protein
KW - mitochondrial DNA (mtDNA)
KW - Holliday junction
KW - mitochondrial nucleoid
N2 - 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.
ER -
BAKKAIOVA, Jana, María Victoria MARINI PALOMEQUE, Smaranda WILLCOX, Jozef NOSEK, Jack D. GRIFFITH, Lumír KREJČÍ and Lubomir TOMASKA. Yeast mitochondrial HMG proteins: DNA-binding properties of the most evolutionarily divergent component of mitochondrial nucleoids. \textit{Bioscience Reports}. London: Portland Press LTD, 2016, vol.~36, No~1, p.~''nestránkováno'', 13 pp. ISSN~0144-8463. Available from: https://dx.doi.org/10.1042/BSR20150275.
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