Mitochondrial helicase Irc3 translocates along double-stranded DNA
| Autor: | Sirelin Sillamaa, Natalja Garber, Juhan Sedman, Ilja Gaidutšik, Vlad–Julian Piljukov, Tiina Sedman, Joosep Paats |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins DNA polymerase DNA polymerase II Biophysics Saccharomyces cerevisiae DNA Mitochondrial Biochemistry 03 medical and health sciences Adenosine Triphosphate Structural Biology Genetics DNA Fungal Molecular Biology chemistry.chemical_classification DNA ligase DNA clamp 030102 biochemistry & molecular biology biology DNA translocase activity Hydrolysis DNA Helicases Helicase Cell Biology Mitochondria Cell biology Kinetics 030104 developmental biology chemistry biology.protein Nucleic Acid Conformation Replisome Primase |
| Zdroj: | FEBS Letters. 591:3831-3841 |
| ISSN: | 0014-5793 |
| Popis: | Irc3 is a superfamily II helicase required for mitochondrial DNA stability in Saccharomyces cerevisiae. Irc3 remodels branched DNA structures, including substrates without extensive single-stranded regions. Therefore, it is unlikely that Irc3 uses the conventional single-stranded DNA translocase mechanism utilized by most helicases. Here we demonstrate that Irc3 disrupts partially triple-stranded DNA structures in an ATP-dependent manner. Our kinetic experiments indicate that the rate of ATP hydrolysis by Irc3 is dependent on the length of the double-stranded DNA cosubstrate. Furthermore, the previously uncharacterized C-terminal region of Irc3 is essential for these two characteristic features and forms a high affinity complex with branched DNA. Together, our experiments demonstrate that Irc3 has double-stranded DNA translocase activity. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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