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Related Concept Videos

Long-patch Base Excision Repair01:02

Long-patch Base Excision Repair

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:
Fixing Double-strand Breaks02:04

Fixing Double-strand Breaks

The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...
Fixing Double-strand Breaks02:04

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The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...
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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
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Nucleotide Excision Repair

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Related Experiment Video

Updated: Jun 2, 2026

Using Modified Synthetic Oligonucleotides to Assay Nucleic Acid-Metabolizing Enzymes
05:33

Using Modified Synthetic Oligonucleotides to Assay Nucleic Acid-Metabolizing Enzymes

Published on: July 5, 2024

FEN nucleases: bind, bend, fray, cut.

R Scott Williams1, Thomas A Kunkel

  • 1Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, DHHS, Research Triangle Park, NC 27709, USA. williamsrs@niehs.nih.gov

Cell
|April 19, 2011
PubMed
Summary
This summary is machine-generated.

Researchers uncovered key molecular mechanisms behind RAD2/FEN nuclease specificities. These findings advance our understanding of DNA replication and maintenance processes.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • The RAD2/FEN nuclease superfamily plays crucial roles in DNA replication and maintenance.
  • Understanding the cleavage specificities of these nucleases is vital for comprehending DNA repair pathways.

Discussion:

  • Orans et al. (2011) and Tsutakawa et al. (2011) provide novel insights into the molecular basis of nuclease activity.
  • The studies highlight the diverse endo- and exonucleolytic cleavage specificities within the RAD2/FEN family.

Key Insights:

  • Detailed molecular principles governing diverse cleavage specificities have been elucidated.
  • The research clarifies how RAD2/FEN nucleases differentiate between various DNA targets.

Outlook:

  • These findings pave the way for future research into DNA repair and replication mechanisms.
  • Further investigation into RAD2/FEN nucleases could lead to therapeutic strategies for diseases related to DNA instability.