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Meiosis I progression in spermatogenesis requires a type of testis-specific 20S core proteasome

Journal article
Authors Qianting Zhang
S. Y. Ji
Kiran Busayavalasa
Jingchen Shao
Chao Yu
Published in Nature Communications
Volume 10
ISSN 2041-1723
Publication year 2019
Published at Department of Chemistry and Molecular Biology
Language en
Links dx.doi.org/10.1038/s41467-019-11346...
Keywords chromosome synapsis, activator pa28, mice lacking, dmc1, complexes, chromatin, histones, failure, repair, genes, Science & Technology - Other Topics, lls nc, 1977, biology of reproduction, v17, p760
Subject categories Developmental Biology

Abstract

Spermatogenesis is tightly regulated by ubiquitination and proteasomal degradation, especially during spermiogenesis, in which histones are replaced by protamine. However, the functions of proteasomal activity in meiosis I and II remain elusive. Here, we show that PSMA8-associated proteasomes are essential for the degradation of meiotic proteins and the progression of meiosis I during spermatogenesis. PSMA8 is expressed in spermatocytes from the pachytene stage, and assembles a type of testis-specific core proteasome. Deletion of PSMA8 decreases the abundance of proteasome in testes. Meiotic proteins that are normally degraded at late prophase I, such as RAD51 and RPA1, remain stable in PSMA8-deleted spermatocytes. Moreover, PSMA8-null spermatocytes exhibit delayed M-phase entry and are finally arrested at this stage, resulting in male infertility. However, PSMA8 is neither expressed nor required for female meiotic progression. Thus, meiosis I progression in spermatogenesis, particularly entry into and exit from M-phase, requires the proteasomal activity of PSMA8-associated proteasomes.

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