Localisation of histone macroH2A1.2 to the XY-body is not a response to the presence of asynapsed chromosome axes

Hoyer‐Fender, Sigrid; Czirr, Eva; Radde, Rebecca; Turner, James M. A.; Mahadevaiah, Shantha K.; Pehrson, John R.; Burgoyne, Paul S.

doi:10.1242/jcs.00851

Cited by 14 publications

(11 citation statements)

References 68 publications

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“…Such findings are consistent with the proposed common, but as yet unknown, mechanisms of heterochromatin formation in both sites. Similar to the present findings, other specific protein and histone modifications implicated in chromatin silencing have been localized to both centromeric and sex chromosome heterochromatin, such as heterochromatin protein-1 (HP-1), histone deacetylases, H3K9, SUV39H1, and macroH2A1.2 (8,10,12,19,20,27,35,38,50).…”

Section: Sumo-1 and Pericentromeric Heterochromatinsupporting

confidence: 89%

SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis

Vigodner¹,

Ishikawa²,

Morris³

2006

American Journal of Physiology-Endocrinology and Metabolism

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Vigodner, Margarita, Tomomoto Ishikawa, Peter N. Schlegel, and Patricia L. Morris. SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis. Am J Physiol Endocrinol Metab 290: E1022-E1033, 2006. First published December 13, 2005 doi:10.1152/ajpendo.00527.2005.-Sumoylation affects multiple cellular events, including chromatin inactivation and transcriptional repression. Our data provide the first characterization of small ubiquitin-related modifier-1 (SUMO-1) expression during human spermatogenesis by the use of high-resolution cellular SUMO-1 bioimaging. During human meiotic prophase, SUMO-1 localizes to sex chromosomes and centromeric and pericentromeric chromatin. As human spermatocytes progress toward the end of prophase in meiosis I, SUMO-1 is no longer detected within the sex body and pericentromeric heterochromatin but localizes exclusively to centromeres. SUMO-1 localization along sex chromosome axes, pseudoautosomal region, and centromeres of both chromosomes supports a role for SUMO-1 sumoylation in epigenetic events occurring over the entire sex body, e.g., meiotic sex chromosome inactivation and chromatin condensation. Centromeric SUMO-1 throughout meiotic prophase suggests a role in centromeric chromatin condensation and/or other centromere/kinetochore functions. SUMO-1 is likely involved in both facultative and constitutive heterochromatin processes in spermatocytes. Haploid round spermatids show a consistent association of SUMO-1 with centromeric clusters. During spermatid elongation, SUMO-1 localizes in the manchette perinuclear ring. Steroidogenic Leydig cells show some cytoplasmic but strong nuclear and perinuclear SUMO-1. Peritubular myoepithelial cell SUMO-1 colocalizes with centromeric heterochromatin. In epithelial Sertoli cells, when associated with centromeric heterochromatin, SUMO-1 is adjacent but not colocalized with the nucleolus. Male germ cells demonstrate no SUMO-1 nucleolar association. Human and rodent Sertoli cells consistently show an inverse correlation between androgen receptor (AR) and SUMO-1 expression and compartmentalization. Sertoli cells from certain infertile patients, however, showed greatly decreased SUMO-1 and AR. Our data suggest that human testicular SUMO-1 has specific functions in heterochromatin organization, meiotic centromere function, and gene expression.small ubiquitin-related modifier-1; meiosis; chromatin; centromere; spermatids; Sertoli cells; Sertoli cell-only; maturational arrest; infertility THE SMALL UBIQUITIN-RELATED MODIFIER 1 (SUMO-1) is a member of a family of ubiquitin-related proteins. In contrast to the process of ubiquitination, which is largely but not always associated with proteolytic pathways, sumoylation is instead implicated in cellular events such as protein-protein interactions, nuclear-cytoplasmic transport, and the formation of specific nuclear heterochromatin domains. Thus sumoylation participates in the regulation of transcription and DNA replication and repa...

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Section: Sumo-1 and Pericentromeric Heterochromatinsupporting

confidence: 89%

SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis

Vigodner¹,

Ishikawa²,

Morris³

2006

American Journal of Physiology-Endocrinology and Metabolism

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“…1D) and is the time when inactivation of the X and Y chromosome occurs, forming the sex vesicle ( Fig. 3) (26,27,29). Although there was little H2A.Z in leptotene/zygotene cells, a significant increase in H2A.Z occurred at pachytene being spread throughout the nucleus.…”

Section: H2amentioning

confidence: 99%

“…Phosphorylated H2A.X (16, 60) and macroH2A1.2 (26,27,54,57) participate in the assembly of the X and Y chromosomes into facultative heterochromatin at the onset of MSCI but are removed at later stages. In mature sperm, macroH2A1.2 can no longer be detected (1).…”

mentioning

confidence: 99%

The X and Y Chromosomes Assemble into H2A.Z, Containing Facultative Heterochromatin, following Meiosis

Greaves

Rangasamy

Devoy

et al. 2006

Molecular and Cellular Biology

105

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Spermatogenesis is a complex sequential process that converts mitotically dividing spermatogonia stem cells into differentiated haploid spermatozoa. Not surprisingly, this process involves dramatic nuclear and chromatin restructuring events, but the nature of these changes are poorly understood. Here, we linked the appearance and nuclear localization of the essential histone variant H2A.Z with key steps during mouse spermatogenesis. H2A.Z cannot be detected during the early stages of spermatogenesis, when the bulk of X-linked genes are transcribed, but its expression begins to increase at pachytene, when meiotic sex chromosome inactivation (MSCI) occurs, peaking at the round spermatid stage. Strikingly, when H2A.Z is present, there is a dynamic nuclear relocalization of heterochromatic marks (HP1␤ and H3 di-and tri-methyl K9), which become concentrated at chromocenters and the inactive XY body, implying that H2A.Z may substitute for the function of these marks in euchromatin. We also show that the X and the Y chromosome are assembled into facultative heterochromatic structures postmeiotically that are enriched with H2A.Z, thereby replacing macroH2A. This indicates that XY silencing continues following MSCI. These results provide new insights into the large-scale changes in the composition and organization of chromatin associated with spermatogenesis and argue that H2A.Z has a unique role in maintaining sex chromosomes in a repressed state.

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“…In oocytes of XY Tdym1 mice which have no XY-body or MSCI, macro-H2A1.2 is not associated with the X and Y chromatin besides the pericentromeric heterochromatin and the PARs. This demonstrates that the presence of macroH2A1.2 on the gonosomal chromatin in early pachytene spermatocytes is not simply due to the presence of gonosomal chromatin per se and is also not a response to the presence of asynapsed chromosomal axes (Hoyer-Fender et al, 2004). However, a comparison of the time course for macroH2A1.2 staining of the gonosomal domain in primary spermatocytes with that for histone H4 and ÁH2A.X supported the possibility that macroH2A1.2 concentration to the XY body might largely be a reflection of increasing chromatin condensation (Hoyer-Fender et al, 2004).…”

Section: Histone H2a Variantsmentioning

confidence: 84%

“…In later stages, macroH2A1.2 in addition associates with the centromeric heterochromatin and with the chromocenter in round spermatids (Hoyer-Fender et al, 2000a) that is an association of the centromeric heterochromatin of all chromosomes in mice (Pardue and Gall, 1970). Careful examination of the localisation patterns of macroH2A1.2 in the gonosomal domain of surfacespread meiocytes from male mice revealed, that macroH2A1.2 localizes to all of the X and Y chromatin in early pachytene and then becomes progressively concentrated at the X and Y centromeres and the synapsed pseudoautosomal regions (PAR) Hoyer-Fender et al, 2004). In oocytes of XY Tdym1 mice which have no XY-body or MSCI, macro-H2A1.2 is not associated with the X and Y chromatin besides the pericentromeric heterochromatin and the PARs.…”

Section: Histone H2a Variantsmentioning

confidence: 99%

Molecular aspects of XY body formation

Hoyer‐Fender

2003

Cytogenet Genome Res

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More than a century ago, a densely stained area inside the nucleus of male meiotic cells was described. It was later shown to harbor the sex chromosomes which undergo transcriptional inactivation in conjunction with heterochromatinisation and synapsis to form the XY body. Formation of the XY body is conserved throughout the mammalian phylogenetic tree and is thought to be essential for successful spermatogenesis. However, its biological role as well as the molecular mechanisms underlying XY body formation are still far from being understood. A lot of effort has already been undertaken to characterize components of the XY body and to investigate their functional implications in sex chromatin heterochromatinisation and meiotic sex chromosome inactivation (MSCI). This review gives an overview of those components and their possible implications in XY body formation and function.

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Localisation of histone macroH2A1.2 to the XY-body is not a response to the presence of asynapsed chromosome axes

Cited by 14 publications

References 68 publications

SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis

SUMO-1, human male germ cell development, and the androgen receptor in the testis of men with normal and abnormal spermatogenesis

The X and Y Chromosomes Assemble into H2A.Z, Containing Facultative Heterochromatin, following Meiosis

Molecular aspects of XY body formation

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