Histone variants in rat spermatogonia and primary spermatocytes

Meistrich, Marvin L.; Bucci, Luke R.; Trostle-Weige, P K; Brock, William A.

doi:10.1016/0012-1606(85)90137-x

Cited by 149 publications

(151 citation statements)

References 18 publications

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“…Synthesis of mouse oocyte histone H4 occurs independently of DNA replication during oogenesis (12), and synthesis of testis-specific histones continues during spermatogenesis, long after DNA synthesis for meiosis has finished (4,39,40). A number of histone H1 proteins are also synthesized independently of DNA replication (11), and H1 mRNAs, particularly H1c and H1e mRNA, are present in nondividing cells (41).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Histone H1-binding Protein, NASP, as a Cell Cycle-regulated Somatic Protein

Richardson¹,

Batova²,

Widgren³

et al. 2000

Journal of Biological Chemistry

134

160

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Nuclear autoantigenic sperm protein (NASP), initially described as a highly autoimmunogenic testis and sperm-specific protein, is a histone-binding protein that is a homologue of the N1/N2 gene expressed in oocytes of Xenopus laevis. Here, we report a somatic form of NASP (sNASP) present in all mitotic cells examined, including mouse embryonic cells and several mouse and human tissue culture cell lines. Affinity chromatography and histone isolation demonstrate that NASP from myeloma cells is complexed only with H1, linker histones. Somatic NASP is a shorter version of testicular NASP (tNASP) with two deletions in the coding region arising from alternative splicing and differs from tNASP in its 5 untranslated regions. We examined the relationship between NASP mRNA expression and the cell cycle and report that in cultures of synchronized mouse 3T3 cells and HeLa cells sNASP mRNA levels increase during Sphase and decline in G 2 , concomitant with histone mRNA levels. NASP protein levels remain stable in these cells but become undetectable in confluent cultures of nondividing CV-1 cells and in nonmitotic cells in various body tissues. Expression of sNASP mRNA is regulated during the cell cycle and, consistent with a role as a histone transport protein, NASP mRNA expression parallels histone mRNA expression. NASP, 1 initially described as a highly autoimmunogenic testis and sperm-specific protein, is present in the nucleus of spermatozoa and spermatogenic cells (1-3), hence the name nuclear autoantigenic sperm protein. Previous studies (4) have demonstrated that human NASP contains three functional histone binding sites: site I (amino acids 116 -127), site II, (amino acids 469 -512), and site III (amino acids 211-244). In vitro, recombinant NASP will bind both linker and core histones (4). 2As a histone-binding protein (4, 5), NASP appears to be a homologue of the N1/N2 gene expressed in oocytes of Xenopus laevis (6 -9) because, in addition to the conserved coding regions, there is an almost 60% identity between the 3Ј untranslated regions of rabbit NASP and Xenopus N1/N2 mRNAs (2). In Xenopus oocytes, the non-chromatin-bound core histones H3 and H4 are associated in a complex with N1/N2 (10, 11), providing a mechanism for the storage of histones for DNA replication in the early embryo. Both mouse (12) and sea urchin oocytes (13) also store histones in a non-chromatin-bound form. Other mammalian histone-binding proteins, for example the nucleosome assembly factor NAP-1 (14 -17), the chromatin assembly factor CAF-1 (18 -21), and the transcription proteins HIRA-HIRIP3 (22), not only bind histones but appear to be important for the assembly of chromatin (19,(23)(24)(25)(26). Consequently NASP may be important not only for both the storage and transport of histones but also for the assembly of chromatin.Here, we report a somatic form of NASP (sNASP) present in almost all tissues examined, including mouse embryonic cells and several mouse and human tissue culture cell lines. Interestingly, an analysis of the histones comp...

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Section: Discussionmentioning

confidence: 99%

Characterization of the Histone H1-binding Protein, NASP, as a Cell Cycle-regulated Somatic Protein

Richardson¹,

Batova²,

Widgren³

et al. 2000

Journal of Biological Chemistry

134

160

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“…The height of premeiosis, meiosis I and II and spermiogenesis blocks indicate the respective DNA content. Data from Platz et al (1977), Meistrich et al (1985), and Kim et al (1 987). …”

Section: Nuclear Isolation and Extraction Of Histonesmentioning

confidence: 99%

“…An additional histone variant, H l a (Seyedin and Kistler, 1979), predominates in spermatogonia and early meiotic prophase spermatocytes but is also a minor component in somatic cells of testis and other tissues (Meistrich et al, 1985). Testis-specific histone variants persist through meiosis until the entire complement of somatic, testis-specific, and testis-enriched histones is replaced by more basic, protamine-like proteins in later stages of spermiogenesis (Bucci et al, 1982;Meistrich et al, 1985).…”

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confidence: 99%

Expression of testis‐specific histone genes during the development of rat spermatogenic cells in vitro

Smith

Tres

Kierszenbaum

1992

Developmental Dynamics

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We have used two radiolabeled oligonucleotide probes (TH2B and Hlt), Northern blotting, two-dimensional gel electrophoresis, and autoradiography to study the temporal expression of TH2B and Hlt testis-specific histone genes during the development of rat spermatogenic cells in vitro. These studies were carried out to determine whether meiotic prophase spermatocytes, known to synthesize in vivo THBB and Hlt histones among other histones, are capable of expressing these testis-specific genes in vitro during an extended period of time. We have found abundant TH2B and Hlt mRNA steady state levels as well as newly-synthesized TH2B and Hlt histones after 5 days of coculture. Northern blots reprobed with Hlt-specific oligonucleotide showed that Hlt mRNA remained prominent when TH2B mRNA started to decline after 8-12 days of coculture. Phase-contrast and transmission electron microscopy studies carried out throughout the course of the experiments demonstrated that the number of viable spermatogonia and meiotic prophase spermatocytes was relatively constant during 12 days of coculture. Spermatocytes, in a clone-like arrangement, remained attached to Sertoli cell surfaces and displayed subcellular features consistent with those observed in the intact seminiferous epithelium. Spermatogonia formed long, branching chains of interconnected cells. Results of this study indicate that spermatogenic cells in coculture with Sertoli cells express testis-specific histone genes for an extended period of time. Testis-specific histone gene expression in vitro should facilitate further studies for understanding the role of these histones in chromatin structure, transcription, and genetic recombination during male meiotic prophase.

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“…During meiotic prophase, striking alterations in chromatin structure occur, and the somatic linker histones are replaced by testis-specific subtype H1t (12)(13)(14). H1t is first detected in mid-pachytene spermatocytes, where it rapidly integrates into the chromatin, replaces most of the other somatic H1 subtypes, and persists until the elongating spermatid stage (15). Surprisingly, knockout of H1t does not affect chromatin remodeling, indicating that other known or unknown linker histones may compensate for its absence (16)(17)(18).…”

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confidence: 99%

HILS1 is a spermatid-specific linker histone H1-like protein implicated in chromatin remodeling during mammalian spermiogenesis

Yan

Burns

et al. 2003

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

165

136

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Chromatin remodeling is a major event that occurs during mammalian spermiogenesis, the process of spermatid maturation into spermatozoa. Nuclear condensation during spermiogenesis is accomplished by replacing somatic histones (linker histone H1 and core histones) and the testis-specific linker histone, H1t, with transition proteins and protamines. It has long been thought that H1t is the only testis-specific linker histone, and that all linker histones are replaced by transition proteins, and subsequently by protamines during spermiogenesis. Here, we report the identification and characterization of a spermatid-specific linker histone H1-like protein (termed HILS1) in the mouse and human. Both mouse and human HILS1 genes are located in intron 8 of the ␣-sarcoglycan genes. HILS1 is highly expressed in nuclei of elongating and elongated spermatids (steps 9 -15). HILS1 displays several biochemical properties that are similar to those of linker histones, including the abilities to bind reconstituted mononucleosomes, produce a chromatosome stop during micrococcal nuclease digestion, and aggregate chromatin. Because HILS1 is expressed in late spermatids that do not contain core histones, HILS1 may participate in spermatid nuclear condensation through a mechanism distinct from that of linker histones. Because HILS1 also belongs to the large winged helix͞forkhead protein superfamily, HILS1 may also regulate gene transcription, DNA repair, and͞or other chromosome processes during mammalian spermiogenesis.spermatogenesis ͉ transition nuclear proteins ͉ in silico subtraction ͉ genome database mining H istones are a family of basic proteins that organize eukaryotic DNA into a compact chromatin. There are five major classes of histones, the core histones H2A, H2B, H3, and H4, and the linker histones, H1. Two of each of the four core histones constitute an octamer unit of the nucleosome particle. H1 histones bind to DNA in the nucleosome and to the linker DNA between nucleosomes, thereby facilitating the compaction of nucleosomes into a 30-nm chromatin fiber and higher-order chromatin structures (1). These interactions between histones and DNA modulate gene activity, and both core and H1 histones have profound effects on transcription (2, 3). Among the five histone classes, H1 histones exhibit the most diversity. In mice and humans, there are eight previously described H1 subtypes, including the five somatic subtypes H1a-H1e, the replacement subtype H1o, the testis-specific linker-histone H1t (4-6), and the oocyte-specific H1 linker histone, H1foo (7). The genomic organizations of these histone H1 genes are conserved (8,9).Spermatogenesis is the process of development of male germ cells from spermatogonia to highly differentiated spermatozoa. During spermatogenesis, chromatin is restructured, and dramatic changes in histone gene expression are observed (10). In spermatogonia and preleptotene spermatocytes (cells undergoing DNA replication), the H1a and H1b linker histones are expressed (11). During meiotic prophase, striking ...

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Histone variants in rat spermatogonia and primary spermatocytes

Cited by 149 publications

References 18 publications

Characterization of the Histone H1-binding Protein, NASP, as a Cell Cycle-regulated Somatic Protein

Characterization of the Histone H1-binding Protein, NASP, as a Cell Cycle-regulated Somatic Protein

Expression of testis‐specific histone genes during the development of rat spermatogenic cells in vitro

HILS1 is a spermatid-specific linker histone H1-like protein implicated in chromatin remodeling during mammalian spermiogenesis

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