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A description of the Mei2-like protein family; structure, phylogenetic distribution and biological context

Daniel C Jeffares1, Matthew J Phillips, Stanley Moore

  • 1Department of Evolutionary Biology, University of Copenhagen, Universitetsparken 15, 2100 Copenhagen, Denmark. djeffares@zi.ku.dk

Development Genes and Evolution
|February 27, 2004
PubMed

Insights

Mei2-like proteins, crucial for meiosis, possess a unique RRM3 domain conserved across eukaryotes. This ancient protein family regulates diverse developmental processes in plants and fungi.

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Genetics

Background:

  • The Schizosaccharomyces pombe Mei2 protein, featuring an RNA recognition motif (RRM), is essential for stimulating meiosis.
  • Mei2 functions by binding non-coding RNA, leading to nuclear accumulation in a "mei2-dot" structure.

Purpose of the Study:

  • To systematically characterize the family of Mei2-like proteins.
  • To investigate the evolutionary conservation and functional divergence of Mei2-like proteins across eukaryotes.

Main Methods:

  • Bioinformatic analysis of protein sequences to identify Mei2-like proteins and their conserved domains.
  • Comparative genomics to determine the distribution of Mei2-like genes in various eukaryotic lineages.

Main Results:

  • Mei2-like proteins represent an ancient eukaryotic family characterized by three RRMs, with a highly conserved C-terminal RRM (RRM3).
  • RRM3 exhibits unique conserved sequence elements and is present in fungi, alveolates (e.g., Paramecium), Entamoeba histolytica, and plants.
  • While RRM3 is conserved between plants and fungi, suggesting conserved molecular mechanisms, plant Mei2-like genes have been co-opted for developmental pattern formation.

Conclusions:

  • Mei2-like proteins are ancient and widespread, with RRM3 serving as a key conserved domain.
  • The study highlights the evolutionary plasticity of Mei2-like proteins, adapting to diverse biological roles while retaining core structural features.

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