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An RNA-Binding Multimer Specifies Nematode Sperm Fate.

Scott T Aoki1, Douglas F Porter1, Aman Prasad1

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.

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|June 28, 2018
PubMed
Summary
This summary is machine-generated.

FOG-3 protein regulates sperm development in C. elegans by binding to thousands of RNAs. This protein multimerizes, enabling it to repress gene expression and control cell fate.

Keywords:
FOG-3RNA binding proteinTob/BTGmultimerizationprotein evolutionsperm fate

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Area of Science:

  • Developmental Biology
  • Molecular Biology
  • Genetics

Background:

  • FOG-3 is a key regulator of sperm fate in C. elegans.
  • It is homologous to mammalian Tob/BTG proteins, known as monomeric RNA-binding adaptors.

Purpose of the Study:

  • To determine the crystal structure of FOG-3.
  • To elucidate the molecular mechanism underlying FOG-3's role in sperm fate specification.
  • To investigate the evolutionary changes in FOG-3 function.

Main Methods:

  • X-ray crystallography to determine FOG-3 structure.
  • In vitro biochemical assays to assess FOG-3 multimerization and RNA binding.
  • RNA-binding analysis in nematode spermatogenic germ cells.
  • Reporter assays to study FOG-3's effect on gene expression.

Main Results:

  • FOG-3 forms dimers that can multimerize, unlike its monomeric mammalian homologs.
  • The multimeric FOG-3 structure exhibits a basic surface, indicating nucleic acid binding.
  • FOG-3 directly binds to nearly 1,000 RNAs, primarily in the 3' UTR, with 94% targeting oogenic mRNAs.
  • FOG-3 represses reporter mRNA expression when tethered.

Conclusions:

  • FOG-3 functions as a multimeric protein to regulate sperm fate in C. elegans.
  • Its mechanism involves direct binding and repression of specific mRNAs.
  • This study reveals the evolution of a protein from a monomeric to a multimeric form with altered function.