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DNA Helicases00:55

DNA Helicases

24.9K
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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Mismatch Repair01:20

Mismatch Repair

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Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
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Homologous Recombination02:31

Homologous Recombination

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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Translesion DNA Polymerases02:10

Translesion DNA Polymerases

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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
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Fixing Double-strand Breaks02:04

Fixing Double-strand Breaks

16.0K
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...
16.0K
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

6.5K
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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Related Experiment Video

Updated: Mar 27, 2026

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
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A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

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DDX3X is a Cl--sensitive RNA helicase.

Ivan Rosa E Silva1, Paula F V do Prado1,2, Felipe Z Benevenutti1

  • 1Brazilian Biosciences National Laboratory (LNBio), Center for Research in Energy and Materials (CNPEM), 13083-970, Campinas, Brazil.

Science Signaling
|March 24, 2026
PubMed
Summary
This summary is machine-generated.

Chloride ions regulate the function of DDX3X, an RNA helicase linked to neurodevelopmental disorders. This interaction impacts stress granule formation and provides insights into disease mechanisms.

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A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

Published on: December 23, 2013

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Area of Science:

  • Molecular Biology
  • Neuroscience
  • Biochemistry

Background:

  • Chloride (Cl-) homeostasis is crucial for neurodevelopment and mature neuronal function.
  • Disruptions in Cl- balance are linked to neurodevelopmental disorders.
  • DDX3X, an RNA helicase involved in stress granule assembly, is associated with neurodevelopmental disorders.

Purpose of the Study:

  • To investigate the role of chloride ions in regulating the function of the DDX3X protein.
  • To explore how Cl- interaction affects DDX3X's ATPase and RNA helicase activities.
  • To understand the impact of a specific DDX3X mutation (R326H) on Cl- sensitivity and neurodevelopmental disorder pathophysiology.

Main Methods:

  • In vitro biochemical assays to assess Cl- interaction with DDX3X's helicase core.
  • Enzyme activity assays (ATPase and RNA helicase) to measure the effect of Cl-.
  • Biomolecular condensation assays to evaluate DDX3X's propensity for stress granule formation.
  • Cellular studies using neuroblastoma cells to observe DDX3X localization and stress granule dynamics.
  • Analysis of the R326H mutation's effect on Cl- binding and function.

Main Results:

  • Chloride ions directly bind to the RNA binding region of the DDX3X helicase core.
  • This interaction impairs DDX3X's ATPase and RNA helicase activities at physiological concentrations.
  • Chloride binding disrupts DDX3X's propensity for biomolecular condensation in vitro.
  • In neuroblastoma cells, Cl- efflux triggers the formation of large, persistent DDX3X stress granules.
  • The R326H mutation disrupts the Cl- binding site, impairing Cl- sensitive functions.

Conclusions:

  • Chloride ion binding is a key regulator of DDX3X protein function.
  • The findings elucidate the molecular mechanisms underlying DDX3X's role in stress granule formation.
  • This study provides critical insights into the pathophysiology of neurodevelopmental disorders linked to DDX3X mutations.