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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Molecular Chaperones and Protein Folding03:00

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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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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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
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G-Quadruplexes act as sequence-dependent protein chaperones.

Adam Begeman1, Ahyun Son1, Theodore J Litberg1

  • 1Department of Chemistry & Biochemistry, Knoebel Institute for Healthy Aging, University of Denver, Denver, CO, USA.

EMBO Reports
|September 18, 2020
PubMed
Summary
This summary is machine-generated.

Nucleic acids, like G-quadruplexes, act as potent chaperones preventing protein aggregation. Their effectiveness is sequence-dependent, offering new insights into cell survival and diseases like ALS.

Keywords:
RNAnucleic acidsprotein aggregationprotein foldingproteostasis

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Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Proteome health is crucial for cellular survival.
  • Nucleic acids demonstrate superior protein aggregation inhibition compared to conventional chaperone proteins.
  • Understanding the molecular mechanisms of nucleic acid chaperone activity is essential.

Purpose of the Study:

  • To investigate the sequence-specific chaperone activity of nucleic acids.
  • To elucidate the role of G-quadruplexes in protein aggregation and cellular environments.
  • To explore the potential of nucleic acids in modulating protein folding and disease pathology.

Main Methods:

  • Evaluation of over 500 nucleic acid sequences for their effects on protein aggregation.
  • Analysis of G-quadruplexes' mechanism of action, including quadruplex:protein oligomerization.
  • Assessment of G-quadruplexes' impact on biosensor protein levels in Escherichia coli (E. coli).

Main Results:

  • The holdase chaperone effect of nucleic acids is demonstrably sequence-dependent.
  • G-quadruplexes effectively prevent protein aggregation through specific oligomerization with proteins.
  • G-quadruplexes were shown to enhance the folded protein levels of a biosensor in E. coli.

Conclusions:

  • Nucleic acids possess inherent sequence-specific chaperone capabilities.
  • G-quadruplexes play a significant role in preventing protein aggregation and maintaining proteome health.
  • These findings link nucleic acid structure to aggregation-related diseases (e.g., fragile X, ALS) and highlight their potential in modulating cellular folding environments.