Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structure and function of argonaute proteins.

Traci M Tanaka Hall1

  • 1Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA. hall4@niehs.nih.gov

Structure (London, England : 1993)
|October 12, 2005
PubMed
Summary

Argonaute (Ago) proteins, known for RNA silencing in eukaryotes, may have similar regulatory roles in prokaryotes. Recent studies reveal their RNA binding and cleavage mechanisms, suggesting functions for prokaryotic Ago proteins.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Enzyme structure and kinetics produce tRNA and nucleotide specificity of Schizosaccharomyces pombe CC- and A-adding enzymes.

Nucleic acids research·2026
Same author

Human pumilio proteins use fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex to repress mRNAs.

The Journal of biological chemistry·2026
Same author

Crystal structures of Caenorhabditis elegans PUF-3 depict plasticity of RNA recognition that enables germline gene regulation.

Nucleic acids research·2026
Same author

Human Pumilio proteins use fuzzy multivalent hydrophobic interactions to recruit the CCR4-NOT deadenylase complex to repress mRNAs.

bioRxiv : the preprint server for biology·2025
Same author

The DND1-NANOS3 complex shapes the primordial germ cell transcriptome via a heptanucleotide sequence in mRNA 3' UTRs.

bioRxiv : the preprint server for biology·2025
Same author

<i>Caenorhabditis elegans</i> FBF-1 and FBF-2 C-terminal intrinsically disordered regions differentially regulate RNA-binding affinity.

RNA (New York, N.Y.)·2025

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Argonaute (Ago) proteins are conserved across prokaryotes and eukaryotes.
  • Eukaryotic Ago proteins are key players in RNA silencing pathways.
  • Prokaryotic Ago protein functions remain largely uncharacterized.

Purpose of the Study:

  • To investigate the potential roles of prokaryotic Argonaute proteins.
  • To elucidate the molecular mechanisms of Argonaute protein function.
  • To provide insights into nucleic acid-directed regulatory pathways.

Main Methods:

  • Structural biology studies of Argonaute proteins.
  • Biochemical assays to determine RNA binding and cleavage activity.
  • Comparative analysis of prokaryotic and eukaryotic Ago proteins.

Related Experiment Videos

Main Results:

  • Recent studies have revealed the structural and biochemical properties of Argonaute proteins.
  • Mechanisms for RNA recognition and cleavage by Ago proteins have been elucidated.
  • These findings suggest potential regulatory functions for prokaryotic Ago proteins.

Conclusions:

  • Argonaute proteins possess conserved RNA-binding and cleavage capabilities.
  • Prokaryotic Ago proteins may participate in nucleic acid-directed regulatory pathways.
  • Further research is warranted to fully understand the functions of prokaryotic Argonaute proteins.