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Unwinding during stressful times: Mechanisms of helicases in meiotic recombination. | LitMetric

Unwinding during stressful times: Mechanisms of helicases in meiotic recombination.

Curr Top Dev Biol

Structural Biochemistry of Meiosis Group, Friedrich Miescher Laboratory of the Max Planck Society, Tuebingen, Germany. Electronic address:

Published: January 2023

AI Article Synopsis

  • - Successful meiosis I relies on proper linkage of homologous chromosomes, primarily achieved through crossovers generated by meiotic recombination, which modifies standard DNA repair processes.
  • - DNA helicases play a crucial role in this process by coupling nucleic acid binding and hydrolysis to alter DNA and protein-DNA substrates necessary for crossover formation.
  • - The review examines the current understanding of meiotic helicases, their interactions, and how regulatory modifications affect their function during meiosis I, emphasizing their molecular structure and mechanisms.

Article Abstract

Successful meiosis I requires that homologous chromosomes be correctly linked before they are segregated. In most organisms this physical linkage is achieved through the generation of crossovers between the homologs. Meiotic recombination co-opts and modifies the canonical homologous recombination pathway to successfully generate crossovers One of the central components of this pathway are a number of conserved DNA helicases. Helicases couple nucleic acid binding to nucleotide hydrolysis and use this activity to modify DNA or protein-DNA substrates. During meiosis I it is necessary for the cell to modulate the canonical DNA repair pathways in order to facilitate the generation of interhomolog crossovers. Many of these meiotic modulations take place in pathways involving DNA helicases, or with a meiosis specific helicase. This short review explores what is currently understood about these helicases, their interaction partners, and the role of regulatory modifications during meiosis I. We focus in particular on the molecular structure and mechanisms of these helicases.

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Source
http://dx.doi.org/10.1016/bs.ctdb.2022.06.004DOI Listing

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