title: A meiotic chromosomal core consisting of cohesin complex proteins recruits DNA recombination proteins and promotes synapsis in the absence of an axial element in mammalian meiotic cells.
abstract: The behavior of meiotic chromosomes differs in several respects from that of their mitotic counterparts, resulting in the generation of genetically distinct haploid cells. This has been attributed in part to a meiosis-specific chromatin-associated protein structure, the synaptonemal complex. This complex consist of two parallel axial elements, each one associated with a pair of sister chromatids, and a transverse filament located between the synapsed homologous chromosomes. Recently, a different protein structure, the cohesin complex, was shown to be associated with meiotic chromosomes and to be required for chromosome segregation. To explore the functions of the two different protein structures, the synaptonemal complex and the cohesin complex, in mammalian male meiotic cells, we have analyzed how absence of the axial element affects early meiotic chromosome behavior. We find that the synaptonemal complex protein 3 (SCP3) is a main determinant of axial-element assembly and is required for attachment of this structure to meiotic chromosomes, whereas SCP2 helps shape the in vivo structure of the axial element. We also show that formation of a cohesin-containing chromosomal core in meiotic nuclei does not require SCP3 or SCP2. Our results also suggest that the cohesin core recruits recombination proteins and promotes synapsis between homologous chromosomes in the absence of an axial element. A model for early meiotic chromosome pairing and synapsis is proposed.
authors.affiliation: Department of Cell and Molecular Biology and Center for Genomics Research, Karolinska Institutet, S-171 77 Stockholm, Sweden.
authors.forename: J
authors.initials: J
authors.lastname: Pelttari
authors.forename: M R
authors.initials: MR
authors.lastname: Hoja
authors.forename: L
authors.initials: L
authors.lastname: Yuan
authors.forename: J G
authors.initials: JG
authors.lastname: Liu
authors.forename: E
authors.initials: E
authors.lastname: Brundell
authors.forename: P
authors.initials: P
authors.lastname: Moens
authors.forename: S
authors.initials: S
authors.lastname: Santucci-Darmanin
authors.forename: R
authors.initials: R
authors.lastname: Jessberger
authors.forename: J L
authors.initials: JL
authors.lastname: Barbero
authors.forename: C
authors.initials: C
authors.lastname: Heyting
authors.forename: C
authors.initials: C
authors.lastname: Höög
mesh_terms: D000818:Animals; D019556:COS Cells; D018797:Cell Cycle Proteins / Q000502:physiology; D002868:Chromosomal Proteins, Non-Histone; D002875:Chromosomes / Q000502:physiology; D004268:DNA-Binding Proteins / Q000502:physiology; D005656:Fungal Proteins; D008540:Meiosis / Q000502:physiology*; D009687:Nuclear Proteins / Q000502:physiology*; D011994:Recombinant Proteins / Q000235:genetics; D013569:Synapses / Q000502:physiology*; D000097722:Cohesins
chemical_list: D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D009687:Nuclear Proteins; D011994:Recombinant Proteins; D000097722:Cohesins; C113093:Sycp2 protein, rat