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Structure and RNA binding of the mouse Pumilio-2 Puf domain

Huw T Jenkins1, Rosanna Baker-Wilding, Thomas A Edwards

  • 1Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.

Journal of Structural Biology
|June 23, 2009
PubMed

Insights

Murine Pumilio 2 (Pum2) protein

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Puf proteins regulate gene expression by binding to messenger RNA (mRNA) 3' untranslated regions.
  • In Drosophila, Pumilio protein is crucial for embryonic patterning via translational repression.
  • Vertebrate Pumilio homologue 2 (Pum2) is involved in germ cell development and interacts with DAZ, DAZL, and BOULE proteins.

Purpose of the Study:

  • To elucidate the structural basis of Pum2's RNA-binding capabilities.
  • To characterize the binding affinity of the Pum2 Puf domain to specific RNA sequences.

Main Methods:

  • X-ray crystallography was used to determine the 1.6Å resolution structure of the murine Pum2 Puf domain.
  • RNA binding assays were performed to assess the affinity of the Pum2 Puf domain for target RNA sequences.

Main Results:

  • The crystal structure of the Pum2 Puf domain was determined at 1.6Å resolution.
  • The Pum2 Puf domain exhibits nanomolar affinity for RNA sequences, including the hunchback Nanos response element (NRE) and a Pum2 binding element (PBE).

Conclusions:

  • The Pum2 Puf domain possesses a defined structure capable of high-affinity RNA binding.
  • This structural and binding information provides insights into Pum2's role in regulating gene expression, particularly in germ cell development.

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