A Histone Programme during the Life Cycle of the Sea Urchin

Brandt, Wolf F.; Strickland, Walter N.; Strickland, Marie; Carlisle, Lesley; Woods, Derek; Holt, Claus von

doi:10.1111/j.1432-1033.1979.tb12864.x

Cited by 93 publications

(25 citation statements)

References 31 publications

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“…Fish: S&no irideus (rainbow trout) complete sequence [22]. Sea urchin: Parechinus angulosus partial sequence [23]. Wheat germ: Triticum aestivum, three variants partial sequence [48].…”

Section: Elsevierln'orth-holland Biomedical Pressmentioning

confidence: 99%

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et al. 1979

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“…Fish: S&no irideus (rainbow trout) complete sequence [22]. Sea urchin: Parechinus angulosus partial sequence [23]. Wheat germ: Triticum aestivum, three variants partial sequence [48].…”

Section: Elsevierln'orth-holland Biomedical Pressmentioning

confidence: 99%

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et al. 1979

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“…Core histone sequences are remarkably conserved during evolution. Nonetheless, a number of histone variants are known (2)(3)(4). Synthesis of core histone variants is stage-specific during sea urchin development (3,4), tissue-specific in mammals (5), and correlated with erythroid differentiation in Friend leukemia cells (6,7).…”

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confidence: 99%

Drosophila nucleosomes contain an unusual histone-like protein.

Palmer¹,

Snyder²,

Blumenfeld³

1980

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

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Histones are major structural components of the basic repeating subunit of chromatin, the nucleosome (1). Core histone sequences are remarkably conserved during evolution. Nonetheless, a number of histone variants are known (2-4). Synthesis of core histone variants is stage-specific during sea urchin development (3, 4), tissue-specific in mammals (5), and correlated with erythroid differentiation in Friend leukemia cells (6, 7). These observations suggest that nucleosome heterogeneity is related to the functional specialization of specific elements of chromatin. In this context, it may be important that mononucleosomes isolated from Drosophila chromatin contain large amounts of a histone-like protein that is not a standard core histone. This protein was first identified by Alfageme et al. (8), and designated D2, or "Drosophila 2."In this communication, we demonstrate that D2 is nucleosomal and histone-like, yet is readily distinguished from each of the four "standard" core histones. It is also conserved during the evolution of Drosophila. The curious features of D2 raise questions about histone evolution and the organization of histone genes in Drosophila.MATERIALS AND METHODS Purification of Nuclei. D. melanogaster embryo nuclei and adult head nuclei were prepared with three modifications of published procedures (9, 10): (i) buffer A of Hewish and Burgoyne (11), containing 1 mM EDTA, 0.2 mM ethylene glycol bis(f3-aminoethyl ether)-N,N,N'N'-tetraacetic acid (EGTA), and 0.2 mM phenylmethylsulfonyl fluoride was used for the nuclear isolation; (ii) the crude nuclear pellet was washed in buffer containing 0.1% Triton X-100; (iii) the detergent-washed nuclei were then resuspended and recentrifuged three times in buffer lacking Triton X-100.Purification of Mononucleosomes. Nuclei were suspended in buffer A of Hewish and Burgoyne (11), made 4 mM in CaCl2, and digested at 250C to 25-29% acid solubility with staphylococcal nuclease (EC 3.1.31.1). Digested nuclei were lysed according to Noll and Kornberg (12). Digests were fractionated by sedimentation through linear (5-20%) sucrose gradients containing 0.5 M NaCl (13) or by electrophoresis in 5% acrylamide gels (14).Analysis of Nucleosomal DNA. DNA was extracted from pooled, sucrose-gradient-purified nucleosomes (15), omitting RNase treatment. DNA was released from electrophoretically purified nucleosomes with 1% NaDodSO4 and proteinase K at 100 ,ug/ml. DNA was electrophoresed on 5% acrylamide slab gels (16) and visualized by staining with ethidium bromide.Analysis of Nucleosomal Proteins. Gradient-purified nucleosomes were precipitated with 10 mM MgCl2 (17) and extracted with protamine/urea/acetic acid (18). The released chromosomal proteins were applied directly to acetic acid/ urea/Triton DF-16 gels (see below). Electrophoretically purified nucleosomes were electrophoresed into dialysis bags and extracted with 0.25 M HCO (8). The extracted proteins were analyzed by two-dimensional electrophoresis (see below). Purification of Histones. D. melanogaster embryo histones w...

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“…2) is short in the histones from sea urchin embryo, mollusc and starfish whereas in the sea urchin sperm cell it is 26-28 residues longer, with the histone from If these findings concern a protein encoded in the DNA as a single copy or as reiterated identical genes, they would be difficult to reconcile with the criteria defining the phylum of echinodermata. However, we have shown previously [26,27] that a multiplicity of variants of H1, H2A and H2B histones does exist in one organism and that therefore the many gene copies [28] in their entirety are not solely the result of the reiteration of identical genes but also of the presence of families of closely related structures. Furthermore, the expression of these genes occurs according to an ontogenetic programme [27].…”

Section: Discussionmentioning

confidence: 99%

“…If the ontogenetic histone programme [21,27,29, 301 does represent at the molecular level the analogy to the morphological events during ontogenesis, namely a recapitulation of the phylogenetic past [31], then it is not surprising that the starfish'sperm histone H2B described here is more closely related to the phylogenetically older somatic mollusc H2B [32] from a different phylum and the embryo H2B [26] of the phylogenetically younger sea urchin than to the corresponding histone from the fully differentiated homologous cell of the adult sea urchin.…”

Section: Discussionmentioning

confidence: 99%

The Histone H2B from the Sperm Cell of the Starfish Marthasterias glacialis

Strickland

Holt

1980

European Journal of Biochemistry

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A single species of histone H2B with a blocked N-terminus has been isolated from sperm of the starfish Marthasterias glacialis. The amino-terminal region of the histone H2BM,,tkastrrLaa shows no similarity to the multiple forms of histones H2B found in the sperm of sea urchins, but there are distinct homologies to the histone of Patella granatina and that of the embryo of Purechinus angulosus. The sequence of the 90 carboxy terminal amino acids is highly conserved as in the other histones H2B.From the sperm cells of three sea urchin species (Parechinus angulosus, Psammechinus miliaris and Echinolampas crassa) we have previously isolated seven histones H2B with distinctly different primary structures which appear to be species-specific [l -41. These histones in their N-terminal regions are characterized by repetitive pentapeptide sequences varying in the nature of the pentapeptide and the degree of reiteration.In order to establish whether these histones H2B with the extended N-terminal region consisting of repeat structures have evolved also in other echinoderms living under similar ecological conditions, we have isolated the histone complement of the star fish Marthasterias glacialis and investigated the histone H2B fraction.Contrary to the sea urchin, the star fish sperm cells contain only a single species of histone H2B.

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A Histone Programme during the Life Cycle of the Sea Urchin

Cited by 93 publications

References 31 publications

More histone structures

More histone structures

Drosophila nucleosomes contain an unusual histone-like protein.

The Histone H2B from the Sperm Cell of the Starfish Marthasterias glacialis

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