J 2016

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

PEVALA, Vladimír; Dominika TRUBAN; Jacob A. BAUER; Július KOŠŤAN; Nina KUNOVÁ et. al.

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

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

References:

Impact factor

Impact factor: 10.162

RIV identification code

RIV/00216224:14110/16:00087823

Organization unit

Faculty of Medicine

UT WoS

000373723100031

EID Scopus

2-s2.0-84971221673

Keywords in English

protein Mgm101; linear mitochondrial genome

Tags

Tags

International impact, Reviewed
Changed: 24/3/2021 10:15, Mgr. Tereza Miškechová

Abstract

V originále

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 project
Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26629S, research and development project
Name: SUMO a stability genomu
Investor: Czech Science Foundation