
We identify a new mammalian cohesin subunit, RAD21-like protein (RAD21L), with sequence similarity to RAD21 and REC8. RAD21L localizes along axial elements in early meiotic prophase, in a manner that is spatiotemporally different to either REC8 or RAD21. Remarkably, RAD21L and REC8 have symmetrical, mutually exclusive localization on the not-yet-synapsed homologues, implying that the cohesin patterning could provide a code for homologue recognition. RAD21 transiently localizes to axial elements after the dissociation of RAD21L and REC8 in late pachytene, a period of recombination repair. Further, we show that the removal of cohesins and synaptonemal complex during late meiotic prophase is promoted by Polo-like kinase 1, which is similar to the mitotic prophase pathway.
Chromosomal Proteins, Non-Histone, Scientific Reports, Centromere, Molecular Sequence Data, Nuclear Proteins, Cell Cycle Proteins, Protein Serine-Threonine Kinases, Phosphoproteins, Chromosomes, Mammalian, Prophase, Mass Spectrometry, DNA-Binding Proteins, Chromosome Pairing, Meiosis, Mice, Protein Subunits, Chromosome Segregation, Proto-Oncogene Proteins, Animals, Amino Acid Sequence, Chromatography, Liquid
Chromosomal Proteins, Non-Histone, Scientific Reports, Centromere, Molecular Sequence Data, Nuclear Proteins, Cell Cycle Proteins, Protein Serine-Threonine Kinases, Phosphoproteins, Chromosomes, Mammalian, Prophase, Mass Spectrometry, DNA-Binding Proteins, Chromosome Pairing, Meiosis, Mice, Protein Subunits, Chromosome Segregation, Proto-Oncogene Proteins, Animals, Amino Acid Sequence, Chromatography, Liquid
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