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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Single-Strand DNA Binding Proteins01:03

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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...
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Genomic DNA in Prokaryotes00:46

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The genome of most prokaryotic organisms consists of double-stranded DNA organized into one circular chromosome in a region of cytoplasm called the nucleoid. The chromosome is tightly wound, or supercoiled, for efficient storage. Prokaryotes also contain other circular pieces of DNA called plasmids. These plasmids are smaller than the chromosome and often carry genes that confer adaptive functions, such as antibiotic resistance.
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Conjugated Proteins02:50

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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
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Genomic DNA in Eukaryotes00:58

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Eukaryotes have large genomes compared to prokaryotes. To fit their genomes into a cell, eukaryotic DNA is packaged extraordinarily tightly inside the nucleus. To achieve this, DNA is tightly wound around proteins called histones, which are packaged into nucleosomes that are joined by linker DNA and coil into chromatin fibers. Additional fibrous proteins further compact the chromatin, which is recognizable as chromosomes during certain phases of cell division.
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Updated: Jun 10, 2025

Genome-wide Mapping of Protein-DNA Interactions with ChEC-seq in Saccharomyces cerevisiae
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Extracellular DNA-protein interactions.

Steven D Goodman1

  • 1Abigail Wexner Research Institute at Nationwide Children's Hospital, Center for Microbial Pathogenesis The Ohio State University College of Medicine 700 Children's Drive, WA5021 Columbus, OH 43205, USA.

Current Opinion in Structural Biology
|October 17, 2024
PubMed
Summary
This summary is machine-generated.

Extracellular DNA, stabilized by proteins, forms novel structures in prokaryotes and eukaryotes. These extracellular nucleoprotein complexes, including extracellular chromatin, are crucial for organism survival.

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High-Resolution Mapping of Protein-DNA Interactions in Mouse Stem Cell-Derived Neurons using Chromatin Immunoprecipitation-Exonuclease ChIP-Exo
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Area of Science:

  • Molecular Biology
  • Microbiology
  • Genetics

Background:

  • Intracellular DNA is essential for genetic material storage and cellular processes like replication.
  • Extracellular DNA is abundant and utilized by both prokaryotic and eukaryotic cells for new functions.
  • Proteins are required to stabilize DNA structures, both intracellularly and extracellularly.

Purpose of the Study:

  • To review host and eubacterial extracellular nucleoprotein structures.
  • To discuss the composition, functions, and interactions of these structures.
  • To highlight the biological significance of extracellular DNA structures.

Main Methods:

  • Literature review of host and eubacterial nucleoprotein structures.
  • Analysis of DNA-protein interactions in extracellular environments.
  • Synthesis of current knowledge on extracellular DNA functions.

Main Results:

  • Extracellular DNA forms diverse nucleoprotein structures, analogous to intracellular chromatin.
  • These structures are stabilized by various host and bacterial proteins.
  • Extracellular DNA structures play vital roles in organism survival.

Conclusions:

  • Extracellular DNA and its associated proteins form functional nucleoprotein complexes.
  • These complexes, including extracellular chromatin, are critical for prokaryotic and eukaryotic survival.
  • Further research into these structures will reveal more about their biological importance.