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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
Homologous Recombination02:31

Homologous Recombination

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...
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...
Nucleic Acid Structure01:25

Nucleic Acid Structure

The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...
The DNA Replication Fork01:02

The DNA Replication Fork

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 forks, one in...
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...

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Related Experiment Video

Updated: May 14, 2026

A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1
08:17

A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1

Published on: April 16, 2021

Single-stranded nucleic acids promote SAMHD1 complex formation.

Victoria Tüngler1, Wolfgang Staroske, Barbara Kind

  • 1Children's Hospital, Technical University Dresden, 01307 Dresden, Germany.

Journal of Molecular Medicine (Berlin, Germany)
|February 2, 2013
PubMed
Summary

SAMHD1 protein binds to both RNA and DNA, a crucial function that is impaired in Aicardi-Goutières syndrome. This interaction is essential for SAMHD1

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Related Experiment Videos

Last Updated: May 14, 2026

A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1
08:17

A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1

Published on: April 16, 2021

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

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks
12:19

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks

Published on: November 10, 2016

Area of Science:

  • Molecular Biology
  • Immunology
  • Genetics

Background:

  • SAMHD1 (SAM domain and HD domain-containing protein 1) is a dGTP-dependent triphosphohydrolase.
  • Mutations in SAMHD1 cause Aicardi-Goutières syndrome (AGS), an inflammatory encephalopathy.
  • AGS and systemic lupus erythematosus share characteristics, including interferon-α activation due to self nucleic acids.

Purpose of the Study:

  • To investigate the direct interaction of SAMHD1 with endogenous nucleic acids in situ.
  • To determine the functional domains of SAMHD1 involved in nucleic acid binding and complex formation.
  • To elucidate the role of nucleic acid interaction in SAMHD1 function and its link to AGS.

Main Methods:

  • Fluorescence cross-correlation spectroscopy (FCCS) was employed to study SAMHD1-nucleic acid interactions.
  • Analysis of SAMHD1 complex formation and its dependence on nucleic acid binding.
  • Investigation of mutant SAMHD1 proteins associated with AGS.

Main Results:

  • SAMHD1 directly associates with endogenous ssRNA and ssDNA in situ.
  • Nucleic acid binding and SAMHD1 complex formation are mutually dependent processes.
  • The HD domain and C-terminal region, but not the SAM domain, are critical for nucleic acid interaction and complex formation.

Conclusions:

  • SAMHD1's interaction with nucleic acids is an integral aspect of its function.
  • Impaired nucleic acid binding and complex formation in AGS-associated SAMHD1 mutants highlight the importance of this interaction.
  • This study provides direct evidence linking SAMHD1's nucleic acid binding to its role in preventing autoimmune and inflammatory conditions.