Novel human testis-specific histone H2B encoded by the interrupted gene on the X chromosome

Churikov, Dmitri; Siino, Joseph S.; Svetlova, Maria; Zhang, Kangling; Gineitis, Arūnas; Bradbury, E. M.; Zalensky, Andrei O.

doi:10.1016/j.ygeno.2004.06.001

Cited by 100 publications

(91 citation statements)

References 46 publications

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“…Testis-specific H2B variants, hTSH2B/TH2B and H2BFWT, were found in the sperm nuclei (2,26). H2BFWT was stably incorporated into nucleosomes in vitro and in vivo (27) and was suggested to have telomere-associated function (26). Whereas it remains to be revealed whether sperm chromatin indeed retains H3T nucleosomes, the robust expression of H3T in the testis suggests its presence in the sperm.…”

Section: Discussionmentioning

confidence: 99%

“…These sperm nucleosomes are suggested to have a specific epigenetic function, because they are significantly enriched around developmentally important genes, such as the imprinted gene clusters, microRNA clusters, and HOX gene clusters. Testis-specific H2B variants, hTSH2B/TH2B and H2BFWT, were found in the sperm nuclei (2,26). H2BFWT was stably incorporated into nucleosomes in vitro and in vivo (27) and was suggested to have telomere-associated function (26).…”

Section: Discussionmentioning

confidence: 99%

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Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

Tachiwana

Kagawa

Osakabe

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

207

236

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A histone H3 variant, H3T, is highly expressed in the testis, suggesting that it may play an important role in the chromatin reorganization required for meiosis and/or spermatogenesis. In the present study, we found that the nucleosome containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1. The crystal structure of the H3T nucleosome revealed structural differences in the H3T regions on both ends of the central α2 helix, as compared to those of H3.1. The H3T-specific residues (Met71 and Val111) are the source of the structural differences observed between H3T and H3.1. A mutational analysis revealed that these residues are responsible for the reduced stability of the H3T-containing nucleosome. These physical and structural properties of the H3T-containing nucleosome may provide the basis of chromatin reorganization during spermatogenesis.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

Tachiwana

Kagawa

Osakabe

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

207

236

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“…Many efforts to identify sperm proteins have been directed to the nuclear proteins [1,[5][6][7][8], to identify the proteins required for sperm motility [9][10], and in the understanding of the membrane proteins required for capacitation, egg interaction and fertilization [11]. So far, most of the fundamental knowledge on the sperm protein composition has been gained using conventional protein purification and identification strategies [1-6, 12, 13].…”

Section: Introductionmentioning

confidence: 99%

“…The latest data provide substantial evidence for the presence of only up to 15% of the DNA complexed to histones and 85% of the DNA complexed to protamines [4,7]. It was once questioned whether histones were present at all in the human sperm nucleus, and their function is still not fully understood at present [4][5][6][7]. The…”

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confidence: 99%

Proteomic identification of human sperm proteins

Martínez-Heredia¹,

Estanyol²,

Ballescà³

et al. 2006

Proteomics

233

177

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Conventional 1-DE has in the past provided a wealth of information concerning the major sperm proteins. However, so far there are relatively few reports exploiting the potential of the present proteomic tools to identify and to study additional yet-unidentified important proteins present in human spermatozoa. In the present work, 2-DE of proteins extracted from human normozoospermic spermatozoa led to the resolution of over 1000 spots. Subsequent excision from the gels of 145 spots and MALDI-TOF MS analysis allowed the identification of 98 different proteins. The function of these proteins turned out to be energy production (23%), transcription, protein synthesis, transport, folding and turnover (23%), cell cycle, apoptosis and oxidative stress (10%), signal transduction (8%), cytoskeleton, flagella and cell movement (10%), cell recognition (7%), metabolism (6%) and unknown function (11%). As many as 23% of the proteins identified have not been previously described as being expressed in human spermatozoa. The present data provide an important clue towards determining the function of these proteins and opens up the possibility to perform additional experiments.

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“…Characteristic in that it does not undergo polyadenilation at its 3 ' terminal, and it is localized in telomeres of sperm chromosomes. [42] Acetylation of some histones accelerates due to their replacement by their variants.…”

Section: Modification Of Chromatin During Spermatogenesismentioning

confidence: 99%

The role of epigenetics in spermatogenesis

Güneş

Kulac

2014

Turkish Journal of Urology

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Male germ cells have a unique morphology and function to facilitate fertilization. Sperm deoxyribonucleic acid (DNA) is highly condensed to protect the paternal genome during transfer from male to oocyte. Sperm cells undergo extensive epigenetic modifications during differentiation to become a mature spermatozoon. Epigenetic modifications, including DNA methylation, histone modifications, and chromatin remodeling are substantial regulators of spermatogenesis. DNA hypermethylation is associated with gene silencing. Meanwhile, hypomethylation is associated with gene expression. In sperm cells, promoters of developmental genes are highly hypomethylated. Proper DNA methylation is essential for embryo development. Histone modifications are chemical modifications that change the DNA-binding capacity of histones and the accessibility of regulatory factors to the DNA, thereby altering gene expression. Phosphorylation, methylation, acetylation, and ubiquitination are primary modifications of lysine and serine residues on histone tails. In addition to somatic histones, testis-specific histone variants are expressed, including histone H2B in mature sperm. The replacement of histones with protamines is a crucial step in spermatogenesis. Histone hyperacetylation induces a loose chromatin structure and facilitates topoisomerase-induced DNA strand breaks. As a result, histones are replaced with transition proteins. Next, the transition proteins are replaced with protamines that induce compaction of sperm DNA. This review provides an overview of epigenetic changes during spermatogenesis.

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Novel human testis-specific histone H2B encoded by the interrupted gene on the X chromosome

Cited by 100 publications

References 46 publications

Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

Proteomic identification of human sperm proteins

The role of epigenetics in spermatogenesis

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