Structure primaire de l'histone riche en glycine et en arginine isolée de la tumeur de chloroleucémie du Rat

Sáutière, Pierre; Tyrou, D; Moschetto, Y; Biserte, G

doi:10.1016/s0300-9084(71)80165-7

Cited by 24 publications

(8 citation statements)

References 7 publications

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“…Histone IV shows a remarkable preservation of sequence throughout the evolution of eukaryotes and, in addition, has a nonrandom distribution of residues and specific sites of e-N-acetylation and e-Nmethylation (4). Some of these findings were independently substantiated in another laboratory (5), and the sequence studies have now been extended to include Novikoff hepatoma (6), rat (7), and porcine (8) histones IV.…”

mentioning

confidence: 88%

Complete Amino-Acid Sequence of Calf-Thymus Histone III

DeLange

Hooper

Smith

1972

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

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Calf-thymus histone III is a single polypeptide chain of 135 residues (combined molecular weight of 15,324) with alanine at both the amino and carboxyl ends. The N12-terminal region (Residues 1-53) of histone III is strongly basic (net charge of +18) and contains lysines-14 and -23, which are e-N-acetylated in a fraction of the molecules, as well as lysines-9 and -27, which are partially e-N-methylated. The COOH-terminal region (Residues 54-135) is only slightly basic (net charge of +4), contains most of the hydrophobic residues, and has a 29-residue sequence that lacks a basic residue. The two cysteines are in the nonbasic region at positions 96 and 110. A few sequence similarities of calf-thymus histone III with other histones have been noted.Histones are basic proteins complexed with DNA in the nuclei of all eukaryotic organisms. Although the functions of histones have not been precisely delineated, it seems likely that they play an important role in the regulation of transcription and replication, in addition to serving as structural components of chromosomes (1).With the availability of improved methods for the separation of histones from each other and from other nuclear components, structural studies were begun on several histones from various organisms. The sequence of calf-thymus histone IV (f2al, GAR histone), one of the two arginine-rich histones, was completed first (2, 3), and this was soon followed by the sequence of pea-seedling histone IV (4). Histone IV shows a remarkable preservation of sequence throughout the evolution of eukaryotes and, in addition, has a nonrandom distribution of residues and specific sites of e-N-acetylation and e-Nmethylation (4). Some of these findings were independently substantiated in another laboratory (5), and the sequence studies have now been extended to include Novikoff hepatoma (6), rat (7), and porcine (8) histones IV.Although partial sequences of other histones have been reported (1, 9-13), the only other complete sequence reported to date is that of calf-thymus histone HUb2 (f2b) (14,15). We now present the complete amino-acid sequence of calf-thymus histone III (f3), the other arginine-rich histone, and the only histone that contains cysteinyl residues. A preliminary account of some of these studjes has been given (16). METHODSCalf-thymus histone III was prepared by method 2 of Johns (17) and further purified by column chromatography on BioRex 70 (18). The S-carboxymethyl derivative was prepared by reduction and alkylation with iodoacetate (19), and the oxidized derivative was prepared by oxidation with performic acid (20). Tryptic, chymotryptic, and cyanogen bromide peptides were obtained from the derivatized proteins by procedures similar to those described for histone IV (3, 21). Larger peptides were further hydrolyzed with trypsin, chymotrypsin, pepsin, or thermolysin to give smaller fragments. The procedures for sequential Edman degradation, hydrolysis with carboxypeptidases or aminopeptidases, and all other methods have been described (3,19,21)....

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confidence: 88%

Complete Amino-Acid Sequence of Calf-Thymus Histone III

DeLange

Hooper

Smith

1972

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

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“…For the sequence determination of histone H 4 in many organisms, amino acid analysis of peptides in combination with positioning of peptides on the basis of homology with calf H4 has been used, often supported to a limited extent by some overlapping peptides and sequencing of selected peptides for a few residues. This approach has been employed for the amino acid sequence determination of H 4 from human spleen [71, pig [30], rat [31] Novikoff hepatoma [32], cuttle fish [33], sea urchin [4,5], Tetrahymena [6,7] and yeast [8]. For Physarum H 4 we used this approach also and obtained sequencing data and amino acid compositions of overlapping peptides comparable to the studies cited above.…”

Section: Discussionmentioning

confidence: 99%

Acetylation and methylation sites in histone H4 from Physarum polycephalum

Waterborg¹,

Fried²,

Matthews³

1983

European Journal of Biochemistry

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Histone H4 has been isolated and purified from plasmodia of Physarum polycephalum. The four major fragments produced by hydrolysis of H4 by acetic acid were separated and the complete amino acid sequence of two of them was determined. By analogy with calf H4, these peptides are at the C-terminus and give the sequence from residue 68 to the C-terminus (residue 102). In this 35 residue sequence there are two minor differences from calf H4:(i) residue 77 is arginine in Physarum H 4 and lysine in calf H4; (ii) lysine-79 is partially methylated in Physarum. Arginine occurs at position 77 in pea H 4 but the occurrence of methylated lysine at position 79 has not been reported for other species. In the N-terminal region, amino acid compositions of acetic acid, tryptic and chymotryptic peptides indicate that Physarum H 4 and calf H4 have identical sequences from the N-terminus to residue 47. There may be minor differences in the region from residue 46 to residue 67. The sites of acetylation were determined by Edman degradation of acetate-labelled peptide 4 -17 of Physarum H4. Acetylation was observed at positions 5,8, 12, and 16. The only other labelled peptide was the N-terminal peptide, which is not susceptible to Edman degradation and is thus probably a-N-acetylated as in most other organisms. The results confirm the conservation of H4 sequence and place Physarum H 4 in an intermediate position between lower eukaryote H4, such as yeast or Tetrahymena H4, and higher eukaryote H4, such as mammalian H 4 or pea H4.

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“…3, first two peaks in each profile). Since no increase in either of these peaks was observed for cycles [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] and 32-34, only cycles [16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31] were examined by system I. Aspartic acid observed at cycle 22 is probably due to partial deamidation of asparagine and does not necessarily imply molecular heterogeneity at this location. Note the complete absence of a peak in the glutamine profile at residue 27 (30,31), which suggest that the divergence of protists is more ancient than the plant-animal divergence.…”

Section: Discussionmentioning

confidence: 99%

“…Histone H4 is the most highly conserved protein known. The complete sequences of H4 of calf, pea, pig, and rat (1)(2)(3)(4) are identical except for replacements in the pea sequence of isoleucine for valine and arginine for lysine at positions 60 and 77, respectively. Partial sequencing of H4 from other sources (5)(6)(7) has revealed only one additional amino-acid replacement: cysteine for threonine at residue 73 of the sea urchin sequence (7).…”

mentioning

confidence: 99%

Amino-acid sequence of Tetrahymena histone H4 differs from that of higher eukaryotes.

Glover¹,

Gorovsky²

1979

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

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A partial amino-acid sequence of Tetrahymena histone H4 has been determined and differs significantly from the sequence of calf or pea H4. The amino terminus of Tetrahymena H4, unlike that of other H4s so far examined, is not acetylated. Of 66 residues determined, one is a single-residue insertion, one a single-residue deletion, and thirteen are amino-acid replacements with respect to the calf thymus H4 sequence. Most Histone H4 is the most highly conserved protein known. The complete sequences of H4 of calf, pea, pig, and rat (1-4) are identical except for replacements in the pea sequence of isoleucine for valine and arginine for lysine at positions 60 and 77, respectively. Partial sequencing of H4 from other sources (5-7) has revealed only one additional amino-acid replacement: cysteine for threonine at residue 73 of the sea urchin sequence (7). Whether this extreme conservatism extends to H4 of all eukaryotes remains to be seen, but electrophoretic and compositional analyses of H4s from a wide variety of species (8-13) suggest that the sequence of H4 has remained essentially constant during the evolution of most eukaryotic organisms.Histone H4 of Tetrahymena thermophila shares many biochemical features with H4 of higher eukaryotes. The electrophoretic behavior of Tetrahymena H4 both on sodium dodecyl sulfate (NaDodSO4) and on acetic acid/urea polyacrylamide gels is indistinguishable from that of calf thymus H4, and both histones behave similarly in purification procedures involving either exclusion chromatography or differential solubility (14). Several minor differences have been reported, however, in the amino-acid compositions of Tetrahymena and calf H4 (14).We have recently observed that Tetrahymena H4 fails to substitute efficiently for calf H4 in nucleosome reconstitution experiments (15) and complexes less strongly than calf H4 with both calf and Tetrahymena H2B and H3 (16). These observations have led us to investigate the primary structure of this histone. We report here that substantial differences exist between Tetrahymena H4 and H4 of higher eukaryotes. MATERIALS AND METHODSHistone H4 was obtained from T. thermophila, strain B VII. Nuclei were isolated and whole histone was extracted as described (17). Histone H4 was purified by chromatography on Bio-Gel P-60 followed by chromatography on carboxymethyl-cellulose (14). Calf thymus H4 was purified by similar procedures. Purified fractions were dialyzed exhaustively against distilled, deionized H20 and lyophilized. Both proteins were greater than 98% pure as estimated by NaDodSO4/ polyacrylamide gel electrophoresis (18,19).Cleavage at methionine residues was obtained by exposure to 10-to 300-fold molar excess of cyanogen bromide (CNBr) in 70% formic acid for 24 hr at 23°C in the dark. CNBr peptides were analyzed on NaDodSO4/polyacrylamide gels by the method of Laemmli (18) modified as follows: the running gel was 20% acrylamide/1% bisacrylamide, and both running and stacking gels contained 8 M urea.Automated Edman degradations were perform...

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Structure primaire de l'histone riche en glycine et en arginine isolée de la tumeur de chloroleucémie du Rat

Cited by 24 publications

References 7 publications

Complete Amino-Acid Sequence of Calf-Thymus Histone III

Complete Amino-Acid Sequence of Calf-Thymus Histone III

Acetylation and methylation sites in histone H4 from Physarum polycephalum

Amino-acid sequence of Tetrahymena histone H4 differs from that of higher eukaryotes.

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