The Maternal Histone H1 Variant, H1M (B4 Protein), Is the Predominant H1 Histone in Xenopus Pregastrula Embryos

Dworkin‐Rastl, Eva; Kandolf, Harald; Smith, Rosamund C.

doi:10.1006/dbio.1994.1042

Cited by 77 publications

(61 citation statements)

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“…We therefore conclude that xNAP-1 is a linker histone chaperone in Xenopus eggs. NAP-1 binding to linker histones may be specific to early embryos, because B4 is the linker histone subtype specific to early embryonic cells (13)(14)(15), and NAP-1 has been shown to be a chaperone for H2A and H2B in other cells (19,20). However, recent findings that histone H1 binding to chromatin is dynamic in mammalian culture cells (36,37) suggest a role for a similar linker histone chaperone to effect rapid exchange of histone H1 in somatic chromatin.…”

Section: Resultsmentioning

confidence: 99%

“…In Xenopus eggs, the core histones H2A-H2B and H3-H4 stored in the cytoplasm are associated with histone chaperones nucleoplasmin and N1͞N2, respectively (11,12). To investigate whether B4, the linker histone of Xenopus eggs (13)(14)(15), is found complexed to other proteins, egg extract was fractionated by gel filtration (Superose 12), and fractions were probed with Abs to B4. The result showed that B4 contained in egg extract was eluted considerably faster from the column than purified B4 in physiological buffer, whereas it was eluted at the same position as purified B4 in high-salt buffer containing 0.5 M KCl (Fig.…”

Section: Incorporation Of Linker Histones Into Dinucleosomesmentioning

confidence: 99%

“…By using egg extracts, we found that B4 (ϭH1X or H1M), the linker histone of Xenopus eggs (13)(14)(15), is associated with nucleosome assembly protein-1 (NAP-1), first identified in mammalian cells as a protein that facilitates the assembly of nucleosome cores in vitro, and has been found in a wide variety of organisms, including yeast, soybean, Drosophila, and humans (16)(17)(18)(19). Several lines of evidence also indicate that NAP-1 functions in vivo as a chaperone for H2A-H2B (19,20).…”

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Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs

Shintomi

Iwabuchi²,

Saeki³

et al. 2005

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

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In eukaryotic cells, genomic DNA is primarily packaged into nucleosomes through sequential ordered binding of the core and linker histone proteins. The acidic proteins termed histone chaperones are known to bind to core histones to neutralize their positive charges, thereby facilitating their proper deposition onto DNA to assemble the core of nucleosomes. For linker histones, however, little has been known about the regulatory mechanism for deposition of linker histones onto the linker DNA. Here we report that, in Xenopus eggs, the linker histone is associated with the Xenopus homologue of nucleosome assembly protein-1 (NAP-1), which is known to be a chaperone for the core histones H2A and Xenopus laevis ͉ chromatosome assembly ͉ cell-free system

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Section: Resultsmentioning

confidence: 99%

Section: Incorporation Of Linker Histones Into Dinucleosomesmentioning

confidence: 99%

mentioning

confidence: 99%

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Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs

Shintomi

Iwabuchi²,

Saeki³

et al. 2005

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

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“…2B}. In this experiment the abundance of histone HI is compared with that of histone B4, because the amount of total B4 protein in the embryo remains constant through gastrulation (i.e., from fertilization to 14 hr postfertilization; Dworkin-Rastl et al 1994). However, because of the rapid increase in the number of embryonic nuclei, the amount of B4 per nucleus decreases during development (Dimitrov et al 1993).…”

Section: Histone Hi Inhibits the Selective Activation Of Chromosomal mentioning

confidence: 99%

Specific regulation of Xenopus chromosomal 5S rRNA gene transcription in vivo by histone H1.

Bouvet

Dimitrov²,

Wolffe³

1994

Genes Dev.

233

154

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The incorporation of histone H1 into chromatin during embryogenesis directs the specific repression of the Xenopus oocyte 5S rRNA genes. An increase in histone H1 content specifically restricts TFIIIA-activated transcription, and a decrease in histone HI within chromatin facilitates the activation of the oocyte 5S rRNA genes by TFIIIA. Variation in the amount of histone HI in chromatin does not significantly influence somatic 5S rRNA gene transcription. Thus, the regulated expression of histone HI during Xenopus development has a specific and dominant role in mediating the differential expression of the oocyte and somatic 5S rRNA genes. This example demonstrates that histones can exert dominant repressive effects on the transcription of a gene in vivo in spite of an abundance of transcription factors for that gene.

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“…The only exception was the maternal H1M protein of X . laevis (also referred to as B4; Smith et al, 1988;Dworkin-Rastl et al, 1994). The H1M (B4) protein shows not only the highest degree of sequence identity (47%) with the CS H1 protein, but also contains several of its unique amino acid residues (arrowheads; Fig.…”

Section: Ipakgaat-e-kqavks-~s:rtgdkk-r-r~-~-imentioning

confidence: 99%

Isolation and Amino Acid Sequence Analysis Reveal an Ancient Evolutionary Origin of the Cleavage Stage (CS) Histones of the Sea Urchin

Brandt

Schwager

Rodrigues

et al. 1997

European Journal of Biochemistry

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The cleavage stage (CS) H1, H2A, and H2B histones of the sea urchin, which have previously been identified by their distinct electrophoretic mobility on Tritonlacidurea gels, are known to be maternally expressed during oogenesis and have been implicated in chromatin remodeling of the male pronucleus following fertilization. Here, we describe the isolation of these three CS histones by reverse-phase HPLC chromatography. Moreover, a novel CS H3 protein was identified by the same purification procedure. A low incorporation of radioactive amino acids into the CS hiqtones during early development revealed that the bulk of these proteins in the blastula embryo are derived from the maternal pool of the egg. Amino acid analysis, together with the previously described electrophoretic mobilities, unequivocally identified the purified proteins as CS histones. Peptide sequence analysis confirmed the novel nature of the CS variants as they are distantly related to the early, late, and sperm histone subtypes of the sea urchin. The CS H1 protein displays highest sequence similarity with the H1M (B4) histone of Xenopus laevis, indicating that the frog H1M protein may be a vertebrate homologue of the CS HI histone. These data suggest an ancient evolutionary origin and wide distribution of the CS histone variants.

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The Maternal Histone H1 Variant, H1M (B4 Protein), Is the Predominant H1 Histone in Xenopus Pregastrula Embryos

Cited by 77 publications

References 0 publications

Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs

Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs

Specific regulation of Xenopus chromosomal 5S rRNA gene transcription in vivo by histone H1.

Isolation and Amino Acid Sequence Analysis Reveal an Ancient Evolutionary Origin of the Cleavage Stage (CS) Histones of the Sea Urchin

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