Chromosome Research

, Volume 15, Issue 5, pp 591–605

ZMM proteins during meiosis: Crossover artists at work

Authors

  • Audrey Lynn
    • Department of Biological, Geological and Environmental SciencesCleveland State University
  • Rachel Soucek
    • Department of Biological, Geological and Environmental SciencesCleveland State University
    • Department of Biological, Geological and Environmental SciencesCleveland State University
Article

DOI: 10.1007/s10577-007-1150-1

Cite this article as:
Lynn, A., Soucek, R. & Börner, G.V. Chromosome Res (2007) 15: 591. doi:10.1007/s10577-007-1150-1

Abstract

Faithful segregation of homologous chromosomes (homologs) during meiosis depends on chiasmata which correspond to crossovers between parental DNA strands. Crossover forming homologous recombination takes place in the context of the synaptonemal complex (SC), a proteinaceous structure that juxtaposes homologs. The coordination between molecular recombination events and assembly of the SC as a structure that provides global connectivity between homologs represents one of the remarkable features of meiosis. ZMM proteins (also known as the synapsis initiation complex  =  SIC) play crucial roles in both processes providing a link between recombination and SC assembly. The ZMM group includes at least seven functionally collaborating, yet structurally diverse proteins: The transverse filament protein Zip1 establishes stable homolog juxtaposition by polymerizing as an integral component of the SC. Zip2, Zip3, and Zip4 likely mediate protein–protein interactions, while Mer3, Msh4, and Msh5 directly promote steps in DNA recombination. This review focuses on recent insights into ZMM functions in yeast meiosis and draws comparisons to ZMM-related proteins in other model organisms.

Key words

double Holliday junctions meiosis recombination stable strand invasion ZMM proteins

Copyright information

© Springer 2007