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PDS 5 proteins regulate the length of axial elements and telomere integrity during male mouse meiosis
Author(s) -
Viera Alberto,
Berenguer Inés,
RuizTorres Miguel,
Gómez Rocío,
Guajardo Andrea,
Barbero José Luis,
Losada Ana,
Suja José A
Publication year - 2020
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201949273
Subject(s) - cohesin , biology , microbiology and biotechnology , meiosis , mitosis , telomere , chromosome segregation , prophase , germline , genetics , somatic cell , chromosome , dna , gene
Cohesin cofactors regulate the loading, maintenance, and release of cohesin complexes from chromosomes during mitosis but little is known on their role during vertebrate meiosis. One such cofactor is PDS 5, which exists as two paralogs in somatic and germline cells, PDS 5A and PDS 5B, with unclear functions. Here, we have analyzed their distribution and functions in mouse spermatocytes. We show that simultaneous excision of Pds5A and Pds5B results in severe defects during early prophase I while their individual depletion does not, suggesting their functional redundancy. Shortened axial/lateral elements and a reduction of early recombination nodules are observed after the strong depletion of PDS 5A/B proteins. Moreover, telomere integrity and their association to the nuclear envelope are severely compromised. As these defects occur without detectable reduction in chromosome‐bound cohesin, we propose that the dynamic behavior of the complex, mediated by PDS 5 proteins, is key for successful completion of meiotic prophase I.