title: The width of the lateral element of the synaptonemal complex is determined by a multilayered organization of its components.
abstract: The synaptonemal complex (SC) is a proteinaceous structure that holds the homologous chromosomes in close proximity while they exchange genetic material in a process known as meiotic recombination. This meiotic recombination leads to genetic variability in sexually reproducing organisms. The ultrastructure of the SC is studied by electron microscopy and it is observed as a tripartite structure. Two lateral elements (LE) separated by a central region (CR) confer its classical tripartite organization. The LEs are the anchoring platform for the replicated homologous chromosomes to properly exchange genetic material with one another. An accurate assembly of the LE is indispensable for the proper completion of meiosis. Ultrastructural studies suggested that the LE is organized as a multilayered unit. However, no validation of this model has been previously provided. In this ultrastructural study, by using mice with different genetic backgrounds that affect the LE width, we provide further evidence that support a multilayered organization of the LE. Additionally, we provide data suggesting additional roles of the different cohesin complex components in the structure of the LEs of the SC.
authors.affiliation: Laboratorio de Microscopía Electrónica, Facultad de Ciencias, Universidad Nacional Autónoma de México, México DF 04510, México. Electronic address: r_oh@ciencias.unam.mx.
authors.forename: Rosario
authors.initials: R
authors.lastname: Ortiz
authors.affiliation: Department of Cell and Molecular Biology, Karolinska Institutet, Berzelius väg 35, 171 77 Stockholm, Sweden. Electronic address: Anna.Kouznetsova@ki.se.
authors.forename: Anna
authors.initials: A
authors.lastname: Kouznetsova
authors.affiliation: Laboratorio de Microscopía Electrónica, Facultad de Ciencias, Universidad Nacional Autónoma de México, México DF 04510, México. Electronic address: omem@ciencias.unam.mx.
authors.forename: Olga M
authors.initials: OM
authors.lastname: Echeverría-Martínez
authors.affiliation: Laboratorio de Microscopía Electrónica, Facultad de Ciencias, Universidad Nacional Autónoma de México, México DF 04510, México. Electronic address: vazqueznin@ciencias.unam.mx.
authors.forename: Gerardo H
authors.initials: GH
authors.lastname: Vázquez-Nin
authors.affiliation: Department of Cell and Molecular Biology, Karolinska Institutet, Berzelius väg 35, 171 77 Stockholm, Sweden. Electronic address: abrahan.hernandez@ki.se.
authors.forename: Abrahan
authors.initials: A
authors.lastname: Hernández-Hernández
mesh_terms: D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism; D002842:Chromatids / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D004268:DNA-Binding Proteins; D008297:Male; D008540:Meiosis; D051379:Mice; D009687:Nuclear Proteins / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D013573:Synaptonemal Complex / Q000378:metabolism* / Q000648:ultrastructure; D000097722:Cohesins
chemical_list: D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D010750:Phosphoproteins; D000097722:Cohesins; C556316:RAD21L protein, mouse; C465863:Rec8 protein, mouse; C490062:Sycp3 protein, mouse
keywords: Electron microscopy; Lateral element width; Meiosis; Synaptonemal complex