PEVALA, Vladimír, Dominika TRUBAN, Jacob A. BAUER, Július KOŠŤAN, Nina KUNOVÁ, Jana BELLOVÁ, Marlene BRANDSTETTER, María Victoria MARINI PALOMEQUE, Lumír KREJČÍ, Ľubomír TOMÁŠKA, Jozef NOSEK and Eva KUTEJOVÁ. The structure and DNA-binding properties of Mgm101 from a yeast with a linear mitochondrial genome. Nucleic Acids Research. Oxford: Oxford University Press, vol. 44, No 5, p. 2227-2239. ISSN 0305-1048. doi:10.1093/nar/gkv1529. 2016.
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Basic information
Original name The structure and DNA-binding properties of Mgm101 from a yeast with a linear mitochondrial genome
Authors PEVALA, Vladimír (703 Slovakia), Dominika TRUBAN (703 Slovakia), Jacob A. BAUER (703 Slovakia), Július KOŠŤAN (40 Austria), Nina KUNOVÁ (703 Slovakia), Jana BELLOVÁ (703 Slovakia), Marlene BRANDSTETTER (40 Austria), María Victoria MARINI PALOMEQUE (858 Uruguay, belonging to the institution), Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution), Ľubomír TOMÁŠKA (703 Slovakia), Jozef NOSEK (703 Slovakia) and Eva KUTEJOVÁ (703 Slovakia).
Edition Nucleic Acids Research, Oxford, Oxford University Press, 2016, 0305-1048.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 10.162
RIV identification code RIV/00216224:14110/16:00087823
Organization unit Faculty of Medicine
Doi http://dx.doi.org/10.1093/nar/gkv1529
UT WoS 000373723100031
Keywords in English protein Mgm101; linear mitochondrial genome
Tags EL OK, podil
Tags International impact, Reviewed
Changed by Changed by: Mgr. Tereza Miškechová, učo 341652. Changed: 24/3/2021 10:15.
Abstract
To study the mechanisms involved in the maintenance of a linear mitochondrial genome we investigated the biochemical properties of the recombination protein Mgm101 from Candida parapsilosis. We show that CpMgm101 complements defects associated with the Saccharomyces cerevisiaemgm101–1ts mutation and that it is present in both the nucleus and mitochondrial nucleoids of C. parapsilosis. Unlike its S. cerevisiae counterpart, CpMgm101 is associated with the entire nucleoid population and is able to bind to a broad range of DNA substrates in a non-sequence specific manner. CpMgm101 is also able to catalyze strand annealing and D-loop formation. CpMgm101 forms a roughly C-shaped trimer in solution according to SAXS. Electron microscopy of a complex of CpMgm101 with a model mitochondrial telomere revealed homogeneous, ring-shaped structures at the telomeric single-stranded overhangs. The DNA-binding properties of CpMgm101, together with its DNA recombination properties, suggest that it can play a number of possible roles in the replication of the mitochondrial genome and the maintenance of its telomeres.
Links
GAP207/12/2323, research and development projectName: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26629S, research and development projectName: SUMO a stability genomu
Investor: Czech Science Foundation
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