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

J 2016

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

BAKKAIOVA, Jana, María Victoria MARINI PALOMEQUE, Smaranda WILLCOX, Jozef NOSEK, Jack D. GRIFFITH et. al.

Základní údaje

Originální název

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

Autoři

BAKKAIOVA, Jana (703 Slovensko), María Victoria MARINI PALOMEQUE (858 Uruguay, domácí), Smaranda WILLCOX (840 Spojené státy), Jozef NOSEK (703 Slovensko), Jack D. GRIFFITH (840 Spojené státy), Lumír KREJČÍ (203 Česká republika, garant, domácí) a Lubomir TOMASKA (703 Slovensko)

Vydání

Bioscience Reports, London, Portland Press LTD, 2016, 0144-8463

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.906

Kód RIV

RIV/00216224:14110/16:00087782

Organizační jednotka

Lékařská fakulta

DOI

http://dx.doi.org/10.1042/BSR20150275

UT WoS

000371296900008

Klíčová slova anglicky

DNA binding protein; DNA compaction; HMG-box containing protein; mitochondrial DNA (mtDNA); Holliday junction; mitochondrial nucleoid

Štítky

EL OK, podil

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 8. 2016 16:19, Ing. Mgr. Věra Pospíšilíková

Anotace

V originále

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.

Návaznosti

GAP207/12/2323, projekt VaV

Název: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I

Investor: Grantová agentura ČR, Endonuleázová a translokázová aktivita v restrikčních-modifikačních komplexech typu I

GA13-26629S, projekt VaV

Název: SUMO a stability genomu

Investor: Grantová agentura ČR, SUMO a stability genomu

Citovat

BAKKAIOVA, Jana, María Victoria MARINI PALOMEQUE, Smaranda WILLCOX, Jozef NOSEK, Jack D. GRIFFITH, Lumír KREJČÍ a 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, roč. 36, č. 1, s. "nestránkováno", 13 s. ISSN 0144-8463. Dostupné z: https://dx.doi.org/10.1042/BSR20150275.

@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 a 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, roč.~36, č.~1, s.~''nestránkováno'', 13 s. ISSN~0144-8463. Dostupné z: https://dx.doi.org/10.1042/BSR20150275.

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