Characterization of Nucleosomes Consisting of the Human Testis/Sperm-Specific Histone H2B Variant (hTSH2B)

Li, Andra; Maffey, Allison H.; Abbott, Wade; Silva, Natalia Conde e; Prunell, Ariel; Siino, Joseph S.; Churikov, Dmitrii; Zalensky, and Andrei O.; Ausió, Juan

doi:10.1021/bi048061n

Cited by 62 publications

(59 citation statements)

References 51 publications

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“…These facts suggested that TSH2B may form an unstable nucleosome for enhanced histone-protamine exchange. Consistently, previous biochemical experiments revealed that human TSH2B does not form a stable histone octamer, although the stabilities of the TSH2B and canonical H2B nucleosomes are similar (Li et al, 2005).…”

Section: Introductionsupporting

confidence: 87%

“…4c,4d,4e,4f,4g,4h,4i and 4j). A previous biochemical study revealed that human TSH2B forms an unstable histone octamer with chicken H2A, H3 and H4 (Li et al, 2005). The water-mediated hydrogen bonds between H2B Asn84 and H4 Arg78 in the canonical nucleosome are not formed in the TSH2B nucleosome.…”

Section: Crystallization and Determination Of The Tsh2b Nucleosome Stmentioning

confidence: 92%

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Structure of human nucleosome containing the testis-specific histone variant TSH2B

Urahama

Horikoshi

Osakabe

et al. 2014

Acta Crystallogr F Struct Biol Commun

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PDB reference: TSH2B nucleosome, 3wkjThe human histone H2B variant TSH2B is highly expressed in testis and may function in the chromatin transition during spermatogenesis. In the present study, the crystal structure of the human testis-specific nucleosome containing TSH2B was determined at 2.8 Å resolution. A local structural difference between TSH2B and canonical H2B in nucleosomes was detected around the TSH2B-specific amino-acid residue Ser85. The TSH2B Ser85 residue does not interact with H4 in the nucleosome, but in the canonical nucleosome the H2B Asn84 residue (corresponding to the TSH2B Ser85 residue) forms watermediated hydrogen bonds with the H4 Arg78 residue. In contrast, the other TSH2B-specific amino-acid residues did not induce any significant local structural changes in the TSH2B nucleosome. These findings may provide important information for understanding how testis-specific histone variants form nucleosomes during spermatogenesis.

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Section: Introductionsupporting

confidence: 87%

Section: Crystallization and Determination Of The Tsh2b Nucleosome Stmentioning

confidence: 92%

Structure of human nucleosome containing the testis-specific histone variant TSH2B

Urahama

Horikoshi

Osakabe

et al. 2014

Acta Crystallogr F Struct Biol Commun

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“…A possible human counterpart of H2AL2, H2A.Bbd, which is highly expressed in the testis, was also suggested to form a specific nucleosome structure with reduced stability (22)(23)(24). Furthermore, nucleosomes containing a testis-specific H2B variant, hTSH2B/TH2B, were reportedly unstable, as compared to the conventional nucleosome (25). Therefore, the instability of these nucleosomes formed by the testis-specific histone variants may be a common property required for chromatin reorganization during spermatogenesis.…”

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.

208

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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“…[2][3][4][5][6][7] Histone variants incorporate into nucleosomes just like canonical histones and the structure of variant nucleosomes is often very similar to that of canonical nucleosomes. 8 Despite that, these molecules clearly have functions that are genetically distinct from canonical histones.…”

Section: Random Deposition Of Histone Variantsmentioning

confidence: 99%

Random deposition of histone variants: A cellular mistake or a novel regulatory mechanism?

Hardy

Robert²

2010

Epigenetics

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Despite the fact that it has been intensively studied during the last decade, the function of the histone variant H2A.Z remains enigmatic. In the last few years, we and others have determined the localization of H2A.Z in various organisms. These studies have revealed that H2A.Z occupies different well defined regions in the genome. Interestingly, H2A.Z occupies the promoters and regulatory regions of active genes, as well as constitutive and facultative heterochromatin. The localization of H2A.Z on genomic regions with so diverse functions suggests that the roles of H2A.Z are multiple, only increasing the mystery around this molecule. The way H2A.Z finds its way into these regions is not fully understood but mechanisms that direct the specific incorporation of H2A.Z in promoters and enhancers have been well described. In this Point of View, we review our recent work suggesting that non-targeted incorporation, coupled to targeted depletion of H2A.Z, is a novel mechanism for localizing H2A.Z to some regions. We propose that the various functions of H2A.Z may be a consequence of the mechanism used for its incorporation, as well as its interactions with other histone variants.

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Characterization of Nucleosomes Consisting of the Human Testis/Sperm-Specific Histone H2B Variant (hTSH2B)

Cited by 62 publications

References 51 publications

Structure of human nucleosome containing the testis-specific histone variant TSH2B

Structure of human nucleosome containing the testis-specific histone variant TSH2B

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

Random deposition of histone variants: A cellular mistake or a novel regulatory mechanism?

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