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Human Argonaute3 has slicer activity.

Mi Seul Park1, Hong-Duc Phan2, Florian Busch1

  • 1Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.

Nucleic Acids Research
|October 18, 2017
PubMed
Summary
This summary is machine-generated.

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Human Argonaute (AGO) proteins play roles in gene silencing. Researchers discovered that AGO3, previously thought to lack cleavage activity, can act as a slicer, but its activity is dependent on specific microRNAs and target RNA sequences.

Area of Science:

  • Molecular Biology
  • RNA Biology
  • Gene Regulation

Background:

  • Human Argonaute (AGO) proteins mediate gene silencing.
  • AGO2 is the only known AGO paralog with slicer activity.
  • AGO1, AGO3, and AGO4 were believed to form slicer-independent complexes.

Purpose of the Study:

  • To investigate the slicer activity of AGO3.
  • To determine the factors influencing AGO3-mediated RNA cleavage.
  • To elucidate the structural basis of AGO3 activity.

Main Methods:

  • Recombinant AGO3 loading with various microRNAs (miRNAs).
  • In vitro RNA cleavage assays using complementary target RNAs.
  • Chimeric guide assays to analyze seed sequence significance.

Related Experiment Videos

  • X-ray crystallography to determine AGO3 structure.

    • Main Results:

    • Recombinant AGO3 exhibits slicer activity with specific miRNAs (e.g., miR-20a), but not others (e.g., let-7a, miR-19b, miR-16).
    • AGO3 slicer activity is dependent on the guide RNA sequence, particularly the post-seed region.
    • Unlike AGO2, AGO3-mediated target cleavage requires both 5' and 3' flanking regions on the target RNA.
    • The crystal structure reveals AGO3 possesses an active site similar to AGO2 but lacks a well-defined nucleic acid-binding channel.

    Conclusions:

    • AGO3 possesses slicer activity, challenging previous assumptions.
    • AGO3's activity is regulated by guide RNA sequence and requires specific substrate flanking regions.
    • The structural data suggests accessory proteins may modulate AGO3's substrate binding and cellular function.