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Cohesin component dynamics during meiotic prophase I in mammalian oocytes
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UNSPECIFIED (2004) Cohesin component dynamics during meiotic prophase I in mammalian oocytes. CHROMOSOME RESEARCH, 12 (3). pp. 197-213. ISSN 0967-3849.
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Abstract
Cohesins are chromosomal proteins that form complexes involved in the maintenance of sister chromatid cohesion during division of somatic and germ cells. Three meiosis-specific cohesin subunits have been reported in mammals, REC8, STAG3 and SMC1beta; their expression in mouse spermatocytes has also been described. Here we studied the localization of different meiotic and mitotic cohesin components during prophase I in human and murine female germ cells. In normal and atretic human fetal oocytes, from leptotene to diplotene stages, REC8 and STAG3 colocalize in fibers. In murine oocytes, SMC1beta, SMC3 and STAG3 are localized along fibers that correspond first to the chromosome axis and then to the synaptonemal complex in pachytene. Mitotic cohesin subunit RAD21 is also found in fibers that decorate the SC during prophase I in mouse oocytes, suggesting a role for this cohesin in mammalian sister chromatid cohesion in female meiosis. We observed that, unlike human oocytes, murine synaptonemal complex protein SYCP3 localizes to nucleoli throughout prophase I stages, and centromeres cluster in discrete locations from leptotene to dictyate. At difference from meiosis in male mice, the cohesin axis is progressively lost during the first week after birth in females with a parallel destruction of the axial elements at dictyate arrest, demonstrating sexual dimorphism in sister chromatid cohesion in meiosis.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH426 Genetics |
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Journal or Publication Title: | CHROMOSOME RESEARCH | ||||
Publisher: | KLUWER ACADEMIC PUBL | ||||
ISSN: | 0967-3849 | ||||
Official Date: | 2004 | ||||
Dates: |
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Volume: | 12 | ||||
Number: | 3 | ||||
Number of Pages: | 17 | ||||
Page Range: | pp. 197-213 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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