The structure and DNA-binding properties of Mgm101 from a yeast with a linear mitochondrial genome

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Publikace nespadá pod Fakultu sportovních studií, ale pod Lékařskou fakultu. Oficiální stránka publikace je na webu muni.cz.
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PEVALA Vladimír TRUBAN Dominika BAUER Jacob A. KOŠŤAN Július KUNOVÁ Nina BELLOVÁ Jana BRANDSTETTER Marlene MARINI PALOMEQUE María Victoria KREJČÍ Lumír TOMÁŠKA Ľubomír NOSEK Jozef KUTEJOVÁ Eva

Rok publikování 2016
Druh Článek v odborném periodiku
Časopis / Zdroj Nucleic Acids Research
Fakulta / Pracoviště MU

Lékařská fakulta

Citace
www https://watermark.silverchair.com/gkv1529.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAAq0wggKpBgkqhkiG9w0BBwagggKaMIIClgIBADCCAo8GCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQM4kUtPj3Aq2Od7asfAgEQgIICYGBChiYEKaG14NNQO0W0Q9TEu--q6Ht1TqTUtnPPPzb_5p
Doi http://dx.doi.org/10.1093/nar/gkv1529
Obor Genetika a molekulární biologie
Klíčová slova protein Mgm101; linear mitochondrial genome
Popis 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.
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