Authors: | Fernandez-Capetillo, O.; Mahadevaiah, S. K.; Celeste, A.; Romanienko, P. J.; Camerini-Otero, R. D.; Bonner, W. M.; Manova, K.; Burgoyne, P.; Nussenzweig, A. |
Article Title: | H2AX is required for chromatin remodeling and inactivation of sex chromosomes in male mouse meiosis |
Abstract: | During meiotic prophase in male mammals, the X and Y chromosomes condense to form a macrochromatin body, termed the sex, or XY, body, within which X- and Y-linked genes are transcriptionally repressed. The molecular basis and biological function of both sex body formation and meiotic sex chromosome inactivation (MSCI) are unknown. A phosphorylated form of H2AX, a histone H2A variant implicated in DNA repair, accumulates in the sex body in a manner independent of meiotic recombination-associated double-strand breaks. Here we show that the X and Y chromosomes of histone H2AX-deficient spermatocytes fail to condense to form a sex body, do not initiate MSCI, and exhibit severe defects in meiotic pairing. Moreover, other sex body proteins, including macroH2A1.2 and XMR, do not preferentially localize with the sex chromosomes in the absence of H2AX. Thus, H2AX is required for the chromatin remodeling and associated silencing in male meiosis. |
Keywords: | controlled study; protein phosphorylation; dna-binding proteins; review; nonhuman; protein localization; animal cell; mouse; spermatocyte; meiosis; mammalia; animals; mice; mice, knockout; spermatocytes; dna repair; animalia; dna strand breakage; nuclear proteins; dna; double stranded dna; genetic recombination; transcription regulation; chromatin; gene repression; x chromosome; protein structure, tertiary; cell nucleus; gene silencing; histone h2a; chromosome pairing; rna polymerase ii; histones; testis; prophase; y chromosome; rad51 recombinase; chromosome inactivation; sex chromosome; sex chromosomes; chromosome condensation; sex chromatin; male; priority journal; sex chromosome aberrations |
Journal Title: | Developmental Cell |
Volume: | 4 |
Issue: | 4 |
ISSN: | 1534-5807 |
Publisher: | Cell Press |
Date Published: | 2003-04-01 |
Start Page: | 497 |
End Page: | 508 |
Language: | English |
DOI: | 10.1016/s1534-5807(03)00093-5 |
PUBMED: | 12689589 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Export Date: 25 September 2014 -- Source: Scopus |