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Related Concept Videos

Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

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, a...
DNA Damage can Stall the Cell Cycle02:36

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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...
DNA Damage Can Stall the Cell Cycle02:36

DNA Damage Can Stall the Cell Cycle

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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.

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Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
06:24

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Published on: February 13, 2019

Regulation of Rad51 function by phosphorylation.

Sonja Flott1, Youngho Kwon, Ying Zhang Pigli

  • 1Department of Biochemistry, Wellcome Trust and Cancer Research UK, Gurdon Institute, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK.

EMBO Reports
|July 9, 2011
PubMed
Summary

Budding yeast Rad51 phosphorylation on Ser 192 by Mec1 kinase is crucial for DNA repair. This modification regulates Rad51

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Rad51 is essential for DNA double-strand break repair via homologous recombination.
  • DNA damage response pathways regulate proteins involved in DNA repair.

Purpose of the Study:

  • To investigate the role of Rad51 phosphorylation in DNA repair.
  • To identify the kinase responsible for Rad51 phosphorylation and its functional consequences.

Main Methods:

  • Site-directed mutagenesis of Rad51 Ser 192.
  • Analysis of DNA damage sensitivity and homologous recombination.
  • In vitro biochemical assays for ATP hydrolysis and DNA binding.

Main Results:

  • Mec1 kinase mediates Rad51 phosphorylation on Ser 192 in response to DNA damage.
  • Mutations at Ser 192 cause hypersensitivity to DNA damage and impaired homologous recombination.
  • Ser 192 is critical for Rad51's ATPase activity and DNA binding in vitro, but not multimer formation.

Conclusions:

  • Mec1-mediated phosphorylation of Rad51 Ser 192 is a key regulatory mechanism for DNA repair by homologous recombination.
  • Phosphorylation at Ser 192 controls Rad51's enzymatic activity and DNA repair function.