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Unconventional conservation reveals structure-function relationships in the synaptonemal complex.

Lisa E Kursel1, Henry D Cope1, Ofer Rog1

  • 1School of Biological Sciences and Center for Cell and Genome Sciences, University of Utah, Salt Lake City, United States.

Elife
|November 17, 2021
PubMed
Summary
This summary is machine-generated.

Protein structure, not just sequence, can be conserved during evolution. This study reveals conserved coiled-coil structures in essential meiotic proteins across diverse species, aiding in identifying new proteins.

Keywords:
C. elegansD. melanogasterP. pacificuscoiled-coilevolutionevolutionary biologygeneticsgenomicshumanindelmeiosissynaptonemal complex

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Genetics

Background:

  • Functional requirements often drive protein sequence conservation.
  • The synaptonemal complex (SC) is crucial for meiosis, aligning chromosomes and regulating genetic exchange.
  • SC proteins exhibit high sequence divergence across species, posing challenges for evolutionary analysis.

Purpose of the Study:

  • To investigate the conservation of secondary structural features in highly divergent meiotic proteins.
  • To explore the role of conserved protein structures in protein evolution and function.
  • To identify novel synaptonemal complex proteins using unconventional conservation signatures.

Main Methods:

  • Analysis of conserved protein length and coiled-coil domain structure in meiotic proteins.
  • Comparative sequence analysis across diverse species including *Caenorhabditis*, *Drosophila*, and mammals.
  • Utilizing conserved structural signatures to identify novel proteins in *Pristionchus pacificus*.

Main Results:

  • SC proteins, despite sequence divergence, show conserved length and coiled-coil domain structures.
  • This conserved structural signature was identified in *Drosophila* and mammals.
  • A novel SC protein, Ppa-SYP-1, was identified in *Pristionchus pacificus* based on these conserved features.

Conclusions:

  • Conserved coiled-coil structures play significant roles in the structure and function of the synaptonemal complex.
  • Expanding sequence analysis beyond per-site similarity enhances understanding of protein evolution.
  • Conserved secondary structures offer a valuable approach for identifying functionally related proteins across species.