Primary Structure of Histone H2A from Gonads of the Starfish <i>Asterias rubens</i>

Martinage, Arlette; Bélaïche, Denise; Dupressoir, Thierry; Sáutière, Pierre

doi:10.1111/j.1432-1033.1983.tb07173.x

Cited by 21 publications

(6 citation statements)

References 27 publications

(12 reference statements)

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“…Much like the major form HI.l, histone subtype H1.2 has a blocked serine residue at the N-terminus, which could be partially unblocked by prolonged digestion with S. aureus V8 proteinase. This peculiar ability of at least some batches of S. aureus V8 proteinase to unblock Nacetylserine has also been reported by others (Martinage et al, 1983;Wouters-Tyrou et al, 1981, and since N-acetylserine is a common N-terminal residue of HI protein we assume that both HI subtypes of C. elegans are blocked by acetylation.…”

Section: Sequence Evidencesupporting

confidence: 83%

The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

Vanfleteren¹,

Bun

Baere³

et al. 1990

Biochemical Journal

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The complete amino acid sequence of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 190 residues and has a blocked N-terminus. Histone subtype H1.2 is 17 residues shorter than the major isoform H1.1, mainly as the result of deletions of short peptide fragments. Considerable divergence from isoform H1.1 has occurred in the N-terminal domain and the very C-terminus of the molecule, but the central globular domain and most of the C-terminal domain, including two potential phosphorylation sites, have been well conserved. Secondary-structure predictions for both H1 isoforms reveal a high potential for helix formation in the N-terminal region 1-33 of isoform H1.1 whereas the corresponding region in isoform H1.2 has low probability of being found in alpha-helix. No major differences in secondary structure are predicted for other parts of both H1 subtypes. The aberrant conformation of isoform H1.2 may be indicative of a significantly different function.

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Section: Sequence Evidencesupporting

confidence: 83%

The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

Vanfleteren¹,

Bun

Baere³

et al. 1990

Biochemical Journal

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“…The limited hydrolysis of the dimer H2A-H2B with the Arg-C endoproteinase yielded two large fragments RP-1 (1 -20) and RP-2 (21 -121), which were separated on Bio-Gel P10 as in [9]. Their amino acid compositions are presented in Table 1.…”

Section: Arg-c Endoproteinase Digestion Of the Dimer H2a-h2bmentioning

confidence: 99%

“…Peptides were eluted with a linear gradient (Waters solvent programm 6) of acetonitrile (0 -30%) in 0.05% trifluoroacetic acid for 30 min. The histone fragments, generated by hydrolysis of the dimer H2A-H2B with Arg-C endoproteinase, were separated by chromatography on a Biogel P10 column (150x 5 cm) equilibrated and eluted with 0.01 M HCl saturated with chloroform [9]. Tryptic peptides of histone H2B were separated by reverse-phase high-pressure liquid chromatography.…”

Section: Sequence Studiesmentioning

confidence: 99%

“…Highly purified histone H2B was isolated by preparative electrophoresis at pH 3.2 in 6.25 M urea [25]. Alternatively, fraction F2b was depleted of histone H2A by acetonic selective precipitation (Martinage, A, unpublished results) and fractionated by chromatography on a Bio Gel PI0 column (1 50 x 5 cm) equilibrated and eluted with 0.01 M HCl saturated with chloroform.The dimer H2A-H2B was obtained from fraction F2b by ion-exchange chromatography on Bio-Rex 70 [9]. …”

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confidence: 99%

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Primary structure of histone H2B from gonads of the starfish Asterias rubens

Martinage

Briand

et al. 1985

European Journal of Biochemistry

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The complete amino acid sequence (121 residues) of histone H2B from gonads of the starfish Asterias rubens has been established from structural data obtained essentially from large fragments generated by cleavage of histone H2B at aspartyl residues and by limited hydrolysis of the dimer H2A-H2B with mouse submaxillary gland protease.No real sequence homology can be found between the amino-terminal sequence (residues 1-21) of starfish and calf H2B. One non-conservative substitution (serine-32 in calf + lysine-28 in starfish) leads to the presence of a cluster of eight basic residues (sequence 23 -30) and to the disappearance of a potential site of phosphorylation.A particular structural feature of starfish histone H2B is the presence of N-dimethylproline at its aminoterminal end. By comparison with N-terminal acetylation, which is commonly found in histones, N-terminal methylation is rarely observed. At the present time the functional significance of the N-terminal methylation as well as that of the proline-rich nature of the amino-terminal sequence of the starfish histone H2B remain to be defined.The amino acid sequences of core particle histones were first determined for calf thymus, then in a variety of tissues and species [l] [21] and found to be located in the N-terminal region.The peculiar structural characteristics and the higher degree of variability observed in histone H2B from Echinidae [I] have led us to investigate the primary structure of histone H2B in Asterinidae, another family of the phylum echinoderms.In this paper we report the complete amino acid sequence of histone H2B from gonads of the starfish Asterias rubens. This sequence was established from structural data provided by tryptic peptides and large fragments derived from cleavage of the protein at aspartic acid and arginine residues.Starfish histone H2B is devoid of a free amino-terminal group. The blocking group has been identified as dimethylproline. The amino-terminal blocking of histones by methylation has only been observed previously in Tetrahymena histone H2B [22]. MATERIALS AND METHODS MaterialsMature starfish were obtained from the Station Marine, Wimereux (France). After excision, gonads were frozen in solid C 0 2 and kept at -20" C until use.Trypsin (treated with TosPheCH2C1) and carboxypeptidases A and B (treated with PhMeS0,F) were obtained from Worthington. Thermolysin was from Merck. Arg-C endoproteinase from mouse submaxillaris gland was purchased from Boehringer.Dimethylallylamine, propan-1 -01, dithioerythritol and anhydrous hydrazine were sequanal grade from Pierce. Benzene and chloro-1 -butane for sequential analysis were purchased from SDS (Peypin, France). Phenylisothiocyanate, heptane and heptafluorobutyric acid were sequanal grade from Merck. Polybrene was purchased from Aldrich and the dipeptide GlyGly from Sigma. All other reagents were of the highest purity available.Isolation of histone H2B and of histone dimer H2A-H2BChromatin was isolated from gonads as described in [23]. The crude fraction F2b was extracted...

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“…Comparison of the sequences of histone H2A from two vertebrate species, one plant and species belonging to several invertebrate phyla The sequences are aligned and numbered up to residue 120 of the calf histone H2A sequence. Sequence data: calf thymus histone H2A (Sautiere et al, 1974); rainbow-trout testis histone H2A (Conner et al, 1984); Drosophila histone H2A (Wells, 1986); starfish (Asterias rubens) gonad histone H2A (Martinage et al, 1983); sea-urchin (Parechinus angulosus) sperm histone H2A (Strickland et al, 1980); cuttlefish (Sepia officinalis) testis histone H2A (Wouters-Tyrou et al, 1982); Sipunculus nudus erythrocyte histone H2A (Kmiecik et al, 1983); wheat-germ histone H2A1 (Rodrigues et al, 1985). differentiate diphenylthiourea from the phenylhydantoin derivative of methionine.…”

mentioning

confidence: 99%

The primary structure of histone H2A from the nematode Caenorhabditis elegans

Vanfleteren¹,

Bun²,

Beeumen³

1987

Biochemical Journal

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The complete primary structure of histone H2A from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 126 amino acid residues and has a blocked N-terminus. By comparison with calf thymus histone H2A, the nematode protein shows five deletions, two insertions and 16 substitutions. Most of the changes occur in the N- and C-terminal regions of the molecule, whereas the central part covering the residues 21-120 is quite well conserved. The lysine residues 5, 8 and 10 were found to be partially acetylated.

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Primary Structure of Histone H2A from Gonads of the Starfish Asterias rubens

Cited by 21 publications

References 27 publications

The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

Primary structure of histone H2B from gonads of the starfish Asterias rubens

The primary structure of histone H2A from the nematode Caenorhabditis elegans

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