Acetylation of rat testis histones H2B and TH2B

doi:10.1016/0012-1606(84)90165-9

Developmental Biology

Volume 101, Issue 2, February 1984, Pages 516-521

https://doi.org/10.1016/0012-1606(84)90165-9 Get rights and content

Abstract

The in vivo acetylation of rat testis histones H3 and H4 has been demonstrated in previous studies. In this study, analysis of purified histone fractions revealed the in vivo acetylation of histone H2B, the testis histone variant designated TH2B, and two or more of the histone H2A variants. These findings are quite significant, because it is possible that all of the core histones are acetylated in elongating spermatids at the time of removal of the entire histone complement for replacement by basic spermatidal transition proteins (S. R. Grimes and N. Henderson, 1983, Arch. Biochem. Biophys. 221, 108–116).

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Lead-mediated inhibition of lysine acetylation and succinylation causes reproductive injury of the mouse testis during development
2020, Toxicology Letters
Citation Excerpt :
Protein posttranslational modifications (PTMs) have been confirmed to be necessary for many important biological processes, such as gene expression, metabolic regulation, and energy production. Abundant studies support that PTMs are important for spermiogenesis, which generally includes meiosis and sperm elongation; for example, histone H4 lysine acetylation (Kac) contributes to the replacement of histones by transition proteins (Tnps) and protamine during sperm elongation (Awe and Renkawitzpohl, 2010; Guan and Yue, 2010), and H3 acetylation co-exists with H4 acetylation in spermiogenesis (Grimes and Henderson, 1984; Hazzouri et al., 2000a). Moreover, our previous studies have confirmed that Kac of cytoplasmic proteins is polarized, which indicates Kac plays necessary roles in meiosis, and high-level lysine succinylation (Ksuc) is identified in elongating sperm (Yang et al., 2018).
Lead (Pb), a widespread heavy metal, may induce serious diseases, particularly male reproductive injury. However, the mechanisms by which Pb induces testicular injury remain unclear. In this paper, we established a mouse model of Pb-induced testicular injury via an intraperitoneal injection of lead chloride at a concentration of 1.5 mg/kg body weight. We confirmed that Pb could induce a series of injuries, including a low litter size, smaller testes, more weak offspring, direct injury, and aberrant spermiogenesis. Our study demonstrated that Pb could inhibit lysine acetylation (Kac) and succinylation (Ksuc) via western blot (WB) and immunofluorescence (IF) analyses. We subsequently separated different germ cells that contained Pre-meiotic spermatogonia (SPG), meiotic spermatocyte (SPC), and round spermatid (RS) into the Pb-treated and control groups and verified that Pb inhibited Kac in SPC, RS, and particularly, during meiosis. Furthermore, our results regarding the inhibition of pyruvate kinase and mitochondrial electron transport chain complex I and II in the Pb-treated groups suggested that Pb may restrain key enzymes to block the TCA cycle and that the low TCA cycle activity could reduce the contents of two important metabolites, acetyl-CoA and succinyl-CoA, to inhibit Kac and Ksuc. Moreover, we examined the influences of the inhibition of Kac and Ksuc on spermiogenesis, which indicated that decreased Kac and Ksuc could impede the replacement of transition proteins in elongating sperm and disorder the distribution of germ cells in the seminiferous tubule. Our research provides novel insights into the mechanisms of Pb reproductive toxicity with respect to lysine acetylation and succinylation.
Cadmium inhibits lysine acetylation and succinylation inducing testicular injury of mouse during development
2018, Toxicology Letters
Citation Excerpt :
Meanwhile, lysine acetylation, as an important PTM, plays a crucial role in the formation of sperm cells. Lysine acetylation of histone H4 is a prerequisite for histones to be replaced by transition nuclear proteins and protamine in spermiogenesis (Awe and Renkawitzpohl, 2010; Bao and Bedford, 2016; Guan and Yue, 2010), and hyperacetylation of H3 was identified to co-exist with H4 hyperacetylation (Grimes and Henderson, 1984; Hazzouri et al., 2000b). Moreover, lysine succinylation closely related to lysine acetylation was identified as a post-translational modification in 2011 (Park et al., 2013; Zhang et al., 2011a), and it also plays a crucial regulatory role in cell differentiation and organismal development (Xie et al., 2012).
The toxic effects of cadmium (Cd) in the reproductive system have been confirmed, and lysine acetylation and succinylation play important roles in spermatogenesis. However, little attention determined whether Cd could affect lysine acylation and how it might have an impact on the reproductive system. Therefore, with the goal of contributing to this subject, we have examined the effects of Cd on lysine acetylation and succinylation of proteins in the germ cells of male mice testes during different developmental stages. We adopted intraperitoneal injection of cadmium chloride (1.2 mg/kg body weight) in mice once every 5 days from postnatal day 5–60. The results showed that Cd could restrict GAPDH activity, ATP and cAMP levels of germ cells to inhibit lysine acetylation and succinylation in the testes, inducing reproductive injuries. Cd also restricts acetylation of histone H4K5 and H4K12, which could result in failure of spermiogenesis. Remarkably, polarized acetylation occurs in meiosis, and high-level acetylation occurs earlier than high-level succinylation during spermatogenesis. Moreover, Cd has a limited effect on body weight but reduces the weight of the testis and litter size. Our research may provide a new way to reveal the mechanisms of Cd reproductive toxicity related to lysine acetylation and succinylation.
Nuclear regulator Pygo2 controls spermiogenesis and histone H3 acetylation
2008, Developmental Biology
Mammalian spermiogenesis, a process where haploid male germ cells differentiate to become mature spermatozoa, entails dramatic morphological and biochemical changes including remodeling of the germ cell chromatin. Proteins that contain one or more plant homeodomain (PHD) fingers have been implicated in the regulation of chromatin structure and function. Pygopus 2 (Pygo2) belongs to a family of evolutionarily conserved PHD finger proteins thought to act as co-activators of Wnt signaling effector complexes composed of β-catenin and LEF/TCF transcription factor. Here we analyze mice containing hypomorphic alleles of pygopus 2 (Pygo2 or mpygo2) and uncover a β-catenin-independent involvement of the Pygo2 protein in spermiogenesis. Pygo2 is expressed in elongating spermatids at stages when chromatin remodeling occurs, and block of Pygo2 function leads to spermiogenesis arrest and consequent infertility. Analysis of spermiogenesis in Pygo2 mutants reveals reduced expression of select post-meiotic genes including protamines, transition protein 2, and H1fnt, all of which are required for germ cell chromatin condensation, and drastically altered pattern of histone H3 hyperacetylation. These findings suggest that Pygo2 is involved in the chromatin remodeling events that lead to nuclear compaction of male germ cells.
Regulated hyperacetylation of core histones during mouse spermatogenesis: Involvement of histone-deacetylases
2000, European Journal of Cell Biology
Here we report a detailed analysis of waves of histone acetylation that occurs throughout spermatogenesis in mouse. Our data showed that spermatogonia and preleptotene spermatocytes contained acetylated core histones H2A, H2B and H4, whereas no acetylated histones were observed throughout meiosis in leptotene or pachytene spermatocytes. Histones remained unacetylated in most round spermatids. Acetylated forms of H2A and H2B, H3 and H4 reappeared in step 9 to 11 elongating spermatids, and disappeared later in condensing spermatids. The spatial distribution pattern of acetylated H4 within the spermatids nuclei, analyzed in 3D by immunofluorescence combined with confocal microscopy, showed a spatial sequence of events tightly associated with chromatin condensation. In order to gain an insight into mechanisms controlling histone hyperacetylation during spermiogenesis, we treated spermatogenic cells with a histone deacetylase inhibitor, trichostatin A (TSA), which showed a spectacular increase of histone acetylation in round spermatids. This observation suggests that deacetylases are responsible for maintaining a deacetylated state of histones in these cells. TSA treatment could not induce histone acetylation in condensing spermatids, suggesting that acetylated core histones are replaced by transition proteins without being previously deacetylated. Moreover, our data showed a dramatic decrease in histone deacetylases in condensing spermatids. Therefore, the regulation of histone deacetylase activity/concentration appears to play a major role in controling histone hyperacetylation and probably histone replacement during spermiogenesis.
The promoter of the poly(A) binding protein 2 (Pabp2) retroposon is derived from the 5'-untranslated region of the Pabp1 progenitor gene
1999, Genomics
The mouse Pabp2 retroposon encodes an isoform of poly(A) binding protein that is expressed in meiotic and early haploid spermatogenic cells. In the present study, we have determined the transcription start site of the Pabp2 gene to clarify the source of its promoter, a prerequisite for expression of retroposons and preservation of their function by natural selection. The 5′ end of the mouse Pabp2 retroposon exhibits extensive similarity to the entire 5′ UTR of the human PABP1 mRNA, but there is no similarity upstream of the transcription start site of the human PABP1 mRNA, indicating that the Pabp2 gene lacks 5′ flanking sequences of the parental PABP1 gene. Oligonucleotide-directed RNase H cleavage and 5′ rapid amplification of cDNA ends both indicate that the transcription start site of the mouse Pabp2 gene is located ∼330 bases downstream of the capsite of the PABP1 mRNA, indicating that the Pabp2 promoter is derived from the PABP1 5′ UTR.
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1991, Progress in Nucleic Acid Research and Molecular Biology
This chapter discusses Bloch's classes Type 1 (“true” protamines) and Type 2 (“stable” protamines), for which substantial molecular information is now available. Protamines are defined as having a cysteine-plus-arginine composition of 45–80 mol% and a serine plus- threonine content of 10–25 mol%. However, it should be mentioned that an additional class of sperm protamines found in the sperm nuclei of certain flat fish in the order Pleuronectiformes. These protamines are rich in arginine and serine, but are very large (80,000–200,000 daltons) compared to the typical true and stable protamines ranging from 5000 to 10,000 Da. In addition, the fact that distinctive amino acids, such as threonine or valine, present in chicken protamine polypeptides, are conserved in position in the amino acid sequence of quail only if the sequence redetermined by Oliva and Dixon is considered, makes the probability of different allelic variants in chicken much less likely.

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^☆: Aided by a grant from the Medical Research Service of the Veterans Administration and by NIH Grant HD 11796.

^☆☆: The research in this paper was made possible by a grant from the Medical Research Service of the Veterans Administration.

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Brief noteAcetylation of rat testis histones H2B and TH2B☆,☆☆

Abstract

Arch. Biochem. Biophys

J. Biol. Chem

Anal. Biochem

Dev. Biol

J. Biol. Chem

J. Biol. Chem

Arch. Biochem. Biophys

Exp. Cell Res

Arch. Biochem. Biophys

Methods Cell Biol

J. Biol. Chem

Prog. Nucleic Acid Res. Mol. Biol

Arch. Biochem. Biophys

Brief note
Acetylation of rat testis histones H2B and TH2B☆,☆☆