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Publication : Identification and molecular characterization of the mammalian α-kleisin RAD21L.

First Author  Gutiérrez-Caballero C Year  2011
Journal  Cell Cycle Volume  10
Issue  9 Pages  1477-87
PubMed ID  21527826 Mgi Jnum  J:173689
Mgi Id  MGI:5050018 Doi  10.4161/cc.10.9.15515
Citation  Gutierrez-Caballero C, et al. (2011) Identification and molecular characterization of the mammalian alpha-kleisin RAD21L. Cell Cycle 10(9):1477-87
abstractText  Meiosis is a fundamental process that generates new combinations between maternal and paternal genomes and haploid gametes from diploid progenitors. Many of the meiosis-specific events stem from the behavior of the cohesin complex (CC), a proteinaceous ring structure that entraps sister chromatids until the onset of anaphase. CCs ensure chromosome segregation, participate in DNA repair, regulate gene expression, and also contribute to synaptonemal complex (SC) formation at meiosis by keeping long-range distant DNA interactions through its conserved structure. Studies from yeast to humans have led to the assumption that Scc1/RAD21 is the alpha-kleisin that closes the tripartite CC that entraps two DNA molecules in mitosis, while its paralog REC8 is essential for meiosis. Here we describe the identification of RAD21L, a novel mammalian CC subunit with homology to the RAD21/REC8 alpha-kleisin subfamily, which is expressed in mouse testis. RAD21L interacts with other cohesin subunits such as SMC1alpha, SMC1b, SMC3 and with the meiosis-specific STAG3 protein. Thus, our results demonstrate the existence of a new meiotic-specific CC constituted by this alpha-kleisin and expand the view of REC8 as the only specific meiotic alpha-kleisin.
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