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DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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The cell cycle is a series of events leading to DNA duplication followed by the division of cell content to form two daughter cells. The cell cycle progresses in four stages—the cell increases in size (gap 1 or G1-phase), duplicates its DNA (synthesis or S-phase), prepares to divide (gap 2 or G2-phase), and divides (mitosis or M-phase).
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An organism’s genome needs to be duplicated in an efficient and error-free manner for its growth and survival. The replication fork is a Y-shaped active region where two strands of DNA are separated and replicated continuously. The coupling of DNA unzipping and complementary strand synthesis is a characteristic feature of a replication fork.   Organisms with small circular DNA, such as E. coli, often have a single origin of replication; therefore, they have only two replication...
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A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases
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A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

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CDK1 phosphorylates WRN at collapsed replication forks.

Valentina Palermo1, Sara Rinalducci2, Massimo Sanchez3

  • 1Section of Experimental and Computational Carcinogenesis, Department of Environment and Health, Istituto Superiore di Sanità, Rome 00161, Italy.

Nature Communications
|September 17, 2016
PubMed
Summary
This summary is machine-generated.

CDK1 phosphorylation of WRN is essential for DNA2-dependent DNA end resection, promoting homologous recombination (HR) repair and chromosome stability. This regulation acts as a switch, directing DNA double-strand break (DSB) repair pathway choice.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Accurate DNA repair pathway choice, switching between homologous recombination (HR) and non-homologous end joining (NHEJ), relies on regulating DNA end-processing.
  • Long-range end resection, a critical step in HR, is poorly understood, particularly its regulation in humans.
  • WRN protein is involved in DNA2 or EXO1-mediated long-range resection pathways.

Purpose of the Study:

  • To investigate the role of WRN phosphorylation by CDK1 in DNA double-strand break (DSB) repair.
  • To elucidate the mechanism by which WRN regulates long-range end resection and its impact on HR and NHEJ.
  • To identify WRN's function as a DSB repair pathway switch.

Main Methods:

  • Investigated the effect of CDK1-mediated WRN phosphorylation on DNA2-dependent end resection at replication-related DSBs.
  • Analyzed WRN phosphorylation site S1133's role in protein relocalization and MRE11 complex interaction.
  • Assessed the impact of impaired WRN phosphorylation on MRE11 foci formation and long-range resection.

Main Results:

  • CDK1 phosphorylation of WRN is crucial for DNA2-dependent end resection, promoting HR, replication recovery, and chromosome stability.
  • S1133 phosphorylation of WRN is not required for foci relocalization but is vital for MRE11 complex interaction.
  • Loss of WRN phosphorylation impairs MRE11 foci formation, inhibits long-range resection, and favors NHEJ at collapsed forks.

Conclusions:

  • CDK1-dependent regulation of WRN-DNA2-mediated resection is unveiled, highlighting a novel mechanism for controlling DNA end-processing.
  • WRN functions as a critical DSB repair pathway switch, with its phosphorylation status dictating the choice between HR and NHEJ.
  • This study provides insights into maintaining genome integrity through precise regulation of DNA repair pathways.