H2A.Bbd: an X-chromosome-encoded histone involved in mammalian spermiogenesis
Toyotaka Ishibashi,Toyotaka Ishibashi,Andra Li,José M. Eirín-López,Ming Zhao,Kristal Missiaen,D. Wade Abbott,D. Wade Abbott,Marvin L. Meistrich,Michael J. Hendzel,Juan Ausió +10 more
TL;DR: The native form of this variant is present in highly advanced spermiogenic fractions of mammalian testis at the time when histones are highly acetylated and being replaced by protamines, providing further support for the functional and structural involvement of this protein in male gametogenesis in mammals.
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Abstract: Despite the identification of H2A.Bbd as a new vertebrate-specific replacement histone variant several years ago, and despite the many in vitro structural characterizations using reconstituted chromatin complexes consisting of this variant, the existence of H2A.Bbd in the cell and its location has remained elusive. Here, we report that the native form of this variant is present in highly advanced spermiogenic fractions of mammalian testis at the time when histones are highly acetylated and being replaced by protamines. It is also present in the nucleosomal chromatin fraction of mature human sperm. The ectopically expressed non-tagged version of the protein is associated with micrococcal nuclease-refractory insoluble fractions of chromatin and in mouse (20T1/2) cell line, H2A.Bbd is enriched at the periphery of chromocenters. The exceedingly rapid evolution of this unique X-chromosome-linked histone variant is shared with other reproductive proteins including those associated with chromatin in the mature sperm (protamines) of many vertebrates. This common rate of evolution provides further support for the functional and structural involvement of this protein in male gametogenesis in mammals.
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Chromatin dynamics during spermiogenesis.
TL;DR: This review highlights the current knowledge on post-meiotic chromatin reorganization and reveals for the first time intriguing parallels in this process in Drosophila and mammals and illustrates the possible mechanisms that lead from a histone-based chromatin to a mainly protamine-based structure during spermatid differentiation.
509
Every amino acid matters: essential contributions of histone variants to mammalian development and disease
TL;DR: An overview of histone variants in the context of their unique functions during mammalian germ cell and embryonic development is provided, and the consequences of aberrant histone variant regulation in human disease are examined.
Histone H2A variants in nucleosomes and chromatin: more or less stable?
Clemens Bönisch,Sandra B. Hake +1 more
TL;DR: Experimental evidence pinpointing towards outstanding roles of these highly variable regions of H2A family members, docking domain, L1 loop and acidic patch are reviewed, and their influence on nucleosome and higher-order chromatin structure and stability is discussed.
Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes
TL;DR: A better understanding of how structural constraints affect protein evolution will greatly help to optimize the authors' models of sequence evolution and the present review explores this new synthesis of perspectives.
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Histone variants in metazoan development
TL;DR: The role of histone variants in the embryo with particular emphasis on early mammalian development is reviewed, suggesting key roles in a number of developmental processes such as the initiation and maintenance of pericentric heterochromatin, X-inactivation, and germ cell differentiation.
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Ming Zhao,Jan Rohozinski,Manju Sharma,Jun Ju,Robert E. Braun,Colin E. Bishop,Marvin L. Meistrich +6 more
TL;DR: It is proposed that when Utp14b initially inserted into Acsl3, it utilized the AcSl3 promoter to drive expression in pachytene spermatocytes to compensate for inactivation of Utp 14a expression, as the protein may have acquired a germ cell-specific function in sperMatid development.
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Kristie L. Rose,Andra Li,Irina Zalenskaya,Yun Zhang,Emmanuel Unni,Kim C. Hodgson,Yaping Yu,Jeffrey Shabanowitz,Marvin L. Meistrich,Donald F. Hunt,Juan Ausió +10 more
TL;DR: It is shown that histones extracted from germ cell populations enriched with spermatids at different stages of development in rat testes reveal an electrophoretic shift in the position of H1t to slower mobilities in elongating sperMatids as compared to that from preceding stages.
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