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Related Concept Videos

Base Excision Repair01:54

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One of the common DNA damages is the chemical alteration of single bases by alkylation, oxidation, or deamination. The altered bases cause mispairing and strand breakage during replication. This type of damage causes minimal change to the DNA double helix structure and can be repaired by the base excision repair (BER) pathways. BER corrects damaged DNA sequences by removing the damaged base and restoring the original base sequence using the complementary strand as a template.
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DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
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Since the discovery of the two BER pathways, there has been a debate about how a cell chooses one pathway over the other and the factors determining this selection. Numerous in vitro experiments have pointed out multiple determinants for the sub-pathway selection. These are:
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In order to be passed through generations, genomic DNA must be undamaged and error-free. However, every day, DNA in a cell undergoes several thousand to a million damaging events by natural causes and external factors. Ionizing radiation such as UV rays, free radicals produced during cellular respiration, and hydrolytic damage from metabolic reactions can alter the structure of DNA. Damages caused include single-base alteration, base dimerization, chain breaks, and cross-linkage.
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Protein-Protein Interactions in DNA Base Excision Repair.

N A Moor1, O I Lavrik

  • 1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia. lavrik@niboch.nsc.ru.

Biochemistry. Biokhimiia
|April 9, 2018
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Summary
This summary is machine-generated.

Base excision repair (BER) maintains genome stability by correcting DNA damage through coordinated protein interactions. Key regulators like XRCC1 and PARP1 scaffold dynamic multiprotein complexes for efficient repair.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Base excision repair (BER) is crucial for correcting abundant DNA damages in mammalian cells, maintaining genome stability.
  • Efficient BER relies on the coordinated action of enzymes and protein factors in a multistage process.
  • Coordination mechanisms involve protein complexes stabilized by direct or DNA-mediated interactions.

Purpose of the Study:

  • This review outlines investigations into direct protein-protein interactions within the BER pathway.
  • It presents known protein partners, interaction sites, and affinity characteristics for key BER participants.
  • The review also discusses regulatory mechanisms of protein interactions, including DNA intermediates and posttranslational modifications.

Main Methods:

  • The review synthesizes findings from studies investigating direct protein-protein interactions in BER.
  • It compiles data on protein partners, interaction sites, and quantitative affinity characteristics.
  • Information on regulatory mechanisms, including DNA-mediated interactions and posttranslational modifications, is presented.

Main Results:

  • Direct interactions between BER proteins and other cellular proteins are detailed.
  • Key protein partners and their interaction sites for main BER participants are identified.
  • Quantitative affinity data for these interactions are provided.

Conclusions:

  • Multiprotein complexes are suggested to form on chromatin, independent of DNA damage, facilitated by XRCC1 and PARP1.
  • These complexes dynamically change composition based on DNA damage type and BER stage.
  • XRCC1 and poly(ADP-ribose) polymerase 1 (PARP1) act as key regulators, scaffolding these dynamic complexes.