Structure and expression of the mouse testicular H1 histone gene (H1t)

Drabent, Birgit; Bode, Christa; Doenecke, Detlef

doi:10.1016/0167-4781(93)90162-7

Cited by 55 publications

(54 citation statements)

References 14 publications

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“…Khadake and Rao (19) compared a mixture of H1 histones (H1b, c, d, and e) and H1t for their ability to decrease the mobility of 5S DNA chromatin using an agarose gel retardation assay and explained the diminished binding of H1t with the lack of S/TPKK motifs in the C terminus. Our finding that the binding behavior to chromatin of histone H1b is similar to that of H1t cannot be explained by the lack of T/SPKK motifs in the C terminus, because H1b has four motifs in the C terminus (44,49).…”

Section: Discussionmentioning

confidence: 72%

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

Talasz

Sapojnikova²,

Helliger

et al. 1998

Journal of Biological Chemistry

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The binding of all known linker histones, named H1a through H1e, including H1 0 and H1t, to a model chromatin complex based on a DNA fragment containing the mouse mammary tumor virus long terminal repeat promotor was systematically studied. As for the histone subtype H1b, we found a dissociation constant of 8 -16 nM to a single mononucleosome (210 base pairs), whereas the binding constant of all other subtypes varied between 2 and 4 nM. Most of the H1 histones, namely H1a, H1c, H1d/e, and H1 0 , completely aggregate polynucleosomes (1.3 kilobase pairs, 6 nucleosomes) at 270 -360 nM, corresponding to a molar ratio of six to eight H1 molecules per reconstituted nucleosome. To form aggregates with the histones H1t and H1b, however, greater amounts of protein were required. Furthermore, our results show that specific types of in vivo phosphorylation of the linker histone tails influence both the binding to mononucleosomes and the aggregation of polynucleosomes. S phase-specific phosphorylation with one to three phosphate groups at specific sites in the C terminus influences neither the binding to a mononucleosome nor the aggregation of polynucleosomes. In contrast, highly phosphorylated H1 histones with four to five phosphate groups in the C and N termini reveal a very high binding affinity to a mononucleosome but a low chromatin aggregation capability. These findings suggest that specific S phase or mitotic phosphorylation sites act independently and have distinct functional roles.H1 histones are a heterogeneous group of at least five subtypes with closely related but nonetheless different primary structures (1, 2). Two further H1 subtypes are known: the histone H1 0 , which is found in nonreplicative tissues (3, 4) and in rapidly proliferating cells (5), and the testis-specific histone variant H1t (6). The various linker histones containing a globular central region flanked by highly basic and hydrophilic C-and N-terminal tails (7,8) bind to the nucleosome and promote the organization of nucleosomes to a higher order structure (9, 10).There is evidence that histone H1 may interact differently with transcriptionally active and inactive regions of chromatin (11). Linker histones are also thought to modulate nucleosome position (12, 13) and to influence replication efficiency in vitro (14).The presence of this large number of various H1 histone subtypes and their possible posttranslational modifications, such as phosphorylation (15), make it very probable that H1 histones play numerous structural and functional roles in chromatin. Until now, no specific role for the various variants has been established although Kaludov et al. (16) showed that the mouse histone H1b binds preferentially to a regulatory sequence within a mouse H3.2 replication-dependent histone gene. Previous analysis of the structural role of H1 histones demonstrated that three subfractions of H1 histones differ in their effectiveness in condensing DNA fibers into ordered aggregates (17) and that histone subtype H1t, compared with other subtypes, dif...

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Section: Discussionmentioning

confidence: 72%

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

Talasz

Sapojnikova²,

Helliger

et al. 1998

Journal of Biological Chemistry

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“…1G,H). To determine whether spermatogenesis became arrested in repro8 mutants before or after the mid-pachytene stage of meiotic prophase, we assessed the presence of histone H1t, a midpachynema marker (Cobb et al, 1999a;Drabent et al, 1993;Inselman et al, 2003). Histone H1t was detected in nuclei of repro8 mutant spermatocytes (see Fig.…”

Section: Resultsmentioning

confidence: 99%

Mutation of Eif4g3, encoding a eukaryotic translation initiation factor, causes male infertility and meiotic arrest of mouse spermatocytes

2010

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The ENU-induced repro8 mutation was identified in a screen to uncover genes that control mouse gametogenesis. repro8 causes male-limited infertility, with failure of spermatocytes to exit meiotic prophase via the G2/MI transition. The repro8 mutation is in the Eif4g3 gene, encoding eukaryotic translation initiation factor 4, gamma 3. Mutant germ cells appear to execute events of meiotic prophase normally, and many proteins characteristic of the prophase-to-metaphase transition are not obviously depleted. However, activity of CDC2A (CDK1) kinase is dramatically reduced in mutant spermatocytes. Strikingly, HSPA2, a chaperone protein for CDC2A kinase, is absent in mutant spermatocytes in spite of the presence of Hspa2 transcript, consistent with the observation that the repro8 phenotype is markedly similar to the phenotype of the Hspa2 knockout. Thus, EIF4G3 is required for HSPA2 translation in spermatocytes, a finding that provides the first genetic evidence for selective translational control of meiotic exit in mammalian spermatocytes.

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“…In spermatogonia and preleptotene spermatocytes, the linker histones H1a and H1b are expressed (6). When cells enter the meiotic prophase, somatic histones are partially replaced by testis-specific core histone variants, including TH2B, TH2A, and tH3 (6 -13) as well as by linker histone variants H1t (14), H1t2 (15), and HILS1 (16).…”

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confidence: 99%

Testis-specific Linker Histone H1t Is Multiply Phosphorylated during Spermatogenesis

Sarg

Chwatal

Talasz

et al. 2009

Journal of Biological Chemistry

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During normal spermatogenesis, the testis-specific linker histone H1t appears at pachytene stage becomes phosphorylated in early spermatids and disappears in late spermatids. Using reversed-phase and hydrophilic interaction liquid chromatography, H1t from rat and mouse testes was isolated, subjected to enzymatic digestion, and analyzed by mass spectrometry. We observed different phosphorylated states of H1t (mono-, di-, and triphosphorylated) as well as the unphosphorylated protein.Tandem mass spectrometry and immobilized metal ion affinity chromatography experiments with MS/MS/MS and multistage activation were utilized to identify five phosphorylation sites on H1t from rats. Phosphorylation occurs on both serine and threonine residues, whereas only two of these sites were located on peptides containing the CDK consensus motif (S/T)PXZ. Rat H1t phosphorylation starts first by phosphorylation of the nonconsensus motif SPKS in the COOH-terminal domain, namely at Ser-140 and to a smaller degree at a further nonconsensus motif at Ser-186. This is followed by phosphorylation of Ser-177 and Thr-155, both located in CDK consensus motifs. A single phosphorylation site at Ser-8 in the NH 2 -terminal tail was also found. Mouse H1t lacks Ser-186 and is phosphorylated at up to four sites. In contrast to somatic linker histones, no strict order of increasing phosphorylation could be detected in H1t. Thus, it appears that not the order of up-phosphorylation but the number of the phosphate groups is necessary for regulated chromatin decondensation, thus facilitating the substitution of H1t by transition proteins and protamines.Mammalian spermatogenesis is a complex, strictly organized process, including proliferation and differentiation. After several mitotic divisions of spermatogonia, germ cells differentiate into spermatocytes and pass through two consecutive meiotic divisions, resulting in haploid round cells termed spermatids. These spermatids then evolve into highly condensed and transcriptionally inert sperm through a process known as spermiogenesis (for a review, see Ref.

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Structure and expression of the mouse testicular H1 histone gene (H1t)

Cited by 55 publications

References 14 publications

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

Mutation of Eif4g3, encoding a eukaryotic translation initiation factor, causes male infertility and meiotic arrest of mouse spermatocytes

Testis-specific Linker Histone H1t Is Multiply Phosphorylated during Spermatogenesis

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