Polycomb protein SCML2 associates with USP7 and counteracts histone H2A ubiquitination in the XY chromatin during male meiosis Journal Article


Authors: Luo, M.; Zhou, J.; Leu, N. A.; Abreu, C. M.; Wang, J.; Anguera, M. C.; De Rooij, D. G.; Jasin, M.; Wang, P. J.
Article Title: Polycomb protein SCML2 associates with USP7 and counteracts histone H2A ubiquitination in the XY chromatin during male meiosis
Abstract: Polycomb group proteins mediate transcriptional silencing in diverse developmental processes. Sex chromosomes undergo chromosome-wide transcription silencing during male meiosis. Here we report that mouse SCML2 (Sex comb on midleg-like 2), an X chromosome-encoded polycomb protein, is specifically expressed in germ cells, including spermatogonia, spermatocytes, and round spermatids. SCML2 associates with phosphorylated H2AX and localizes to the XY body in spermatocytes. Loss of SCML2 in mice causes defective spermatogenesis, resulting in sharply reduced sperm production. SCML2 interacts with and recruits a deubiquitinase, USP7, to the XY body in spermatocytes. In the absence of SCML2, USP7 fails to accumulate on the XY body, whereas H2A monoubiquitination is dramatically augmented in the XY chromatin. Our results demonstrate that the SCML2/USP7 complex constitutes a novel molecular pathway in modulating the epigenetic state of sex chromosomes during male meiosis. © 2015 Luo et al.
Keywords: controlled study; protein expression; unclassified drug; nonhuman; protein function; protein localization; animal cell; mouse; spermatocyte; meiosis; animal tissue; mus; complex formation; apoptosis; protein protein interaction; in vivo study; cell specificity; epigenetics; chromatin; cellular distribution; fetus; histone h2ax; polycomb group protein; spermatogenesis; histone ubiquitination; histone phosphorylation; spermatogonium; spermatid; male; female; article; deubiquitinase; histone gamma h2ax; protein scml2; protein usp7; xy chromatin
Journal Title: PLoS Genetics
Volume: 11
Issue: 1
ISSN: 1553-7390
Publisher: Public Library of Science  
Date Published: 2015-01-29
Start Page: e1004954
Language: English
DOI: 10.1371/journal.pgen.1004954
PROVIDER: scopus
PMCID: PMC4310598
PUBMED: 25634095
DOI/URL:
Notes: Export Date: 2 April 2015 -- Source: Scopus
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  1. Maria Jasin
    249 Jasin