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Updated: Aug 14, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Bioinformatic analyses implicate the collaborating meiotic crossover/chiasma proteins Zip2, Zip3, and Spo22/Zip4 in

Jason Perry1, Nancy Kleckner, G Valentin Börner

  • 1Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.

Proceedings of the National Academy of Sciences of the United States of America
|November 30, 2005
PubMed

Insights

Meiosis proteins Zip2, Zip3, and Spo22 (Zip4) collaborate to form crossovers. Zip3 has ubiquitin E3 ligase features, suggesting a role in protein modification during this crucial cell division process.

Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Zip2 and Zip3 are meiosis-specific proteins essential for crossover and chiasma formation.
  • Their precise molecular functions and interactions remain largely unknown.
  • Understanding these proteins is key to deciphering the mechanisms of meiotic recombination.

Purpose of the Study:

  • To identify functional collaborators of Zip2 and Zip3 in meiosis.
  • To elucidate the molecular roles and structural features of Zip2, Zip3, and Spo22 (Zip4).
  • To characterize the protein domains and evolutionary conservation of these meiosis-specific proteins.

Main Methods:

  • Identification of Spo22 (Zip4) as a potential functional partner of Zip2/3.
  • Structural analysis of Zip3, revealing a RING finger domain characteristic of ubiquitin E3 ligases.
  • Application of the Alignment Based Repeat Annotation (ABRA) tool to identify protein repeat motifs in Zip2 and Spo22/Zip4.

Main Results:

  • Spo22 (Zip4) is identified as a likely collaborator of Zip2 and Zip3.
  • Zip3 possesses a RING finger domain homologous to known ubiquitin E3 ligases, suggesting a role in ubiquitination.
  • Zip2 is characterized as a 14-blade WD40-like repeat protein, and Spo22/Zip4 as a 22-unit tetratricopeptide repeat protein.

Conclusions:

  • Zip2, Zip3, and Zip4 likely function together in a complex.
  • The findings suggest a process involving Zip3-mediated ubiquitin labeling, potentially forming a novel ubiquitin-conjugating complex.
  • These proteins are part of a conserved cohort across related yeast species, highlighting their fundamental role in meiosis.

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