Autor: |
Piljukov, Vlad–Julian, Garber, Natalja, Sedman, Tiina, Sedman, Juhan |
Předmět: |
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Zdroj: |
FEBS Letters; Oct2020, Vol. 594 Issue 19, p3142-3155, 14p |
Abstrakt: |
Irc3 is a superfamily II DNA helicase required for the maintenance of mitochondrial DNA stability in Saccharomyces cerevisiae. Here, we show that recombinant Irc3 is a monomeric protein and that it can form a binary complex with forked DNA. The catalytically active enzyme is a monomer as no positive cooperativity of ATP hydrolysis or DNA unwinding can be detected. Interestingly, we find that Irc3 prefers to unwind the nascent lagging strand at a replication fork. Using DNase I footprinting, we demonstrate that Irc3 captures DNA substrates by establishing a strong contact at the DNA branching point. Additional protections on the lagging strand template suggest a 3′‐to‐5′ polarity for Irc3 movement. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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