The Amino-Acid Sequence of Trout-Testis Histone H1

MacLeod, A. Robert; Wong, Norman C.W.; Dixon, Gordon H.

doi:10.1111/j.1432-1033.1977.tb11739.x

Cited by 103 publications

(25 citation statements)

References 37 publications

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“…Liver and kidney each contained an additional component that migrated more rapidly than the major band of HI in polyacrylamide gels, and which probably corresponds to one or more of the variants observed by Seyedin and Cole [41]. Also consistent with the observations of Macleod et al [42] and Seyedin and Cole [41] was the presence of an homogeneous H1 fraction in trout testis. In erythrocytes, approximately 40% of the total histone H1 was present in a rapidly migrating component previously identified as 'H5' by Miki and Neelin [14].…”

Section: Resultssupporting

confidence: 81%

Use of protein blotting to study the DNA‐binding properties of histone H1 and H1 variants

Wright

Wiersma

Dixon

1987

European Journal of Biochemistry

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Sub-types of histone H1 have been observed in a variety of tissues from several organisms. One of the best characterized H1 variants is H5 from avian erythrocytes. Several lines of evidence suggest that H5 has a greater affinity for DNA than H1 and is thus thought to account, in part, for the highly condensed and transcriptionally repressed state of avian erythrocyte chromatin. In trout there is an analogous erythrocyte-specific HI variant, previously termed 'H5' [B. L. A. Miki and J. M. Neelin (1975) Can. J . Biochem. 53, 1158-1169). Using a sensitive and rapid protein-blotting procedure which is specific amongst the histones for histone H1 and its variants, we compared DNA-binding properties of the trout erythrocyte histone 'H5' and chicken H5. By increasing the NaCl concentration of the binding buffer, a gradual decrease in the amount of DNA that bound to chicken H l , trout HI and trout erythrocyte 'H5' variant was observed, such that at concentrations above 0.37 M, negligible amounts of DNA were bound. By contrast, chicken H5 bound a significantly greater amount of DNA even at a concentration of 0.4 M NaC1. Based on the DNA-binding, properties, we conclude that the trout erythrocyte variant 'H5' is more closely related to H1 than to H5. By assaying the DNA-binding affinity of calf thymus HI peptide fragments, generated by protease and chemical cleavage, and the sperm-specific H1 variants of the annelid, Platynereis dumerilii, which possess greatly shortened C-terminal tails, we conclude that a domain that includes a very small portion of the C-terminal tail and part of the globular domain is sufficient for the binding of H1 to DNA.It is well established that the core histones, H2A, H2B, H3 and H4, are responsible for the primary level of DNA folding, the nucleosome [l, 21. H1 histones are associated with the linker regions between nucleosomes and are generally believed to organize the internucleosomal DNA into higher orders of folding [l -41. The class of lysine-rich histones H1, found in most eucaryotic cells, is the most variable of the live histone classes [4]. Since the multiplicity of H1 is both tissueand species-specific [5 -71, the structural differences among Hls may play a role in determining the degree of chromatin condensation and thereby provide a coarse control of template activity [8].One of the best characterized H1 variants, termed H5, is found in the nucleated erythrocytes of birds [9 -121, amphibians [13], fish [13-161 and possibly reptiles [17]. During the maturation of nucleated erythrocytes there is pronounced condensation of chromatin and genome repression concomitant with the partial replacement of H1 with H5 in the linker regions [14,35,[18][19][20][21][22][23][24][25]. This sequence of events has led to the suggestion that H5 may be the agent of condensation and genome repression and may, therefore, play a fundamental role in the maturation of nucleated erythrocytes.The histones H1 and H5 in avian erythrocytes share a common architecture [26 -291, regions of partial sequence homolog...

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Section: Resultssupporting

confidence: 81%

Use of protein blotting to study the DNA‐binding properties of histone H1 and H1 variants

Wright

Wiersma

Dixon

1987

European Journal of Biochemistry

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“…In rabbit thymus H1 [12] and in calf thymus H1 [13] the aminoterminal 40 residues are rich in alanine, lysine and proline. A similar distribution has been found in the first 26 residues of trout testis H1 [14]. In contrast the amino-terminal random-coil regions of avian H5 histones are shorter and not particularly basic except for a short region from residues 12 to 22 [7].…”

supporting

confidence: 71%

The Primary Structure of Histone H1 from Sperm of the Sea Urchin Parechinus angulosus. 1. Chemical and Enzymatic Fragmentation of the Protein and the Sequence of Amino Acids in the Four N-Terminal Cyanogen Bromide Peptides

Strickland

Groot

et al. 1980

Eur J Biochem

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The primary structure of the amino-terminal 84 residues of sperm histone H1p,,,,,tinus has been determined. The sequence is : Pro -Gly -Ser-Pro-Gln-Lys-Arg -Ala-Ala-Ser-Pro -Arg -Lys-Ser -ProArg -Lys-Ser -Pro -Lys-Lys-Ser-Pro -Arg-Lys -Ala-Ser -Ala-Ser -Pro -Arg -Arg -Lys -Ala-Lys -ArgAla-Arg -Ala-Ser-Thr -Of the five major species of histones found in most eukaryotic organisms, histone H1 is the only one that does not form part of the core particle structure of the chromosome [ l -51. Histones H1 may be involved in the higher-order structure of chromosomes since they are active agents in salt-induced chromatin condensation [6].Histones H5 found in erythrocytes of birds and reptiles have many homologies in their amino acid sequences to histone H1 [7]. Histones H1 and H5 are the most variable among the histones and in many cases H1 histones show species and tissue specificity [8,9]. In general H1 and H5 histones appear to consist of three domains [lo, 111. At the amino-terminal end there is a variable length of random coil. In rabbit thymus H1 [12] and in calf thymus H1 [13] the aminoterminal 40 residues are rich in alanine, lysine and proline. A similar distribution has been found in the first 26 residues of trout testis H1 [14]. In contrast the amino-terminal random-coil regions of avian H5 histones are shorter and not particularly basic except for a short region from residues 12 to 22 [7]. Following the variable-sized amino-terminal random coil there is a hydrophobic region of approximately 80 residues in all H1 and H5 species whose structures have been studied [12-151. This region has a low basic amino acid content, few alanine residues and no proline, and probably exists in vivo as a globular region [lo, 111. At the carboxyl end of all H1 species studied, there are regions of approximately 100 residues with a very high content of lysine, alanine and proline. The same situation occurs in H5 proteins except that, in addition, there are a large number of arginine residues present. A group of lysine, arginine, alanine-rich histones from sperm cells of marine invertebrates [16,17] have been studied. These proteins have been called dsl proteins, but no information on their primary structure is available. The ds1 protein from the sea urchin Arbacia lixula has an almost identical amino acid composition to that of histone H1 from sperm cells of Parechinus angulosus as described in the present paper. Puigdomenech et al. [17] further conclude that the arginine residues in the ds protein are located at both ends of the molecule. Most of the arginine residues of Parechinus HI histone are also located at both ends of the molecule (see also the following paper [18]). In the present paper the purification and isolation of the protein and peptides of the entire protein and the amino acid sequence of the NHz-terminal 84 residues are reported, while the complete primary structure is reported and its unique features are discussed in the following paper [ 181. MATERIALS AND METHODS MaterialsCollection of sperm cells, cold stor...

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“…Amino ucid anulysis of the globulur subunit 9fPhysarurn polycephalum H I Thc first column gives values for P. polycephalum H1 globular subunit obtained from combined amino acid analysis and N M R data fit; values in parentheses arc normalised to 7 histidines. Values in the second column arc for calf thymus H1 globular subunit from the sequence [33] (normalised to 1 tyrosine), in the third for P. polycephalum H1 N-terminal chymotryptic peptide by amino acid analysis [Z], in the fourth calf thymus H1 N-terminal peptide by amino acid analysis from sequence 1-106 [49] ( u , h ) , non-structured conditions ( 2 H 2 0 , pH 2 ) and (c, d) .structured conditions j 2 H 2 0 / l M NuC 'I, p H 8.8) The binding of Physwum H1 to DNA and DNA-cellulosc as observed by ultraviolet absorption and correlated with binding behaviour of calf thymus H1 [6,37,381 show very similar results to the gross effects observed in this paper.…”

Section: N a Binding Studiesmentioning

confidence: 99%

Physical studies by NMR and circular dichroism determining three structurally different domains in Physarum polycephalum histone H1

1985

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Combined studies which include, NMR spectroscopy, circular dichroism, amino acid analysis and polyacrylamide gel electrophoresis together show that the protein designated as histone H1 from Physarum polycephulum has many of the features of histone H1 derived from other sources. The molecular masses of the globular peptide and the whole molecule were found to be 9000 & 1000 Da and 33000 NMR melting experiments showed that the half-melt temperature was 53 & 1 "C and the enthalpy of melting was 100 kJ . mol-'. Unusual facets of the molecule are the relatively large numbers of histidine residues (6 or 7) and the mono, di and trimethylation of some of the lysines, the major type of modification being trimethylation of 9 & 2 residues. The conditions necessary for structuring Physarum HI are not the same as the histone H1 from calf thymus. It is suggested that titration of the histidine residues is the most decisive step for the development of tertiary folding of the globular unit. Da respectively.The histones in Physururn polycephalum were first tentatively assigned by Mohberg and Rush in 1969 [I], but it was not until 1983 that histones H2B and H3 were clearly distinguished [2]. No primary sequence data of histone H1 from P. polycephalum is available at present, but it has been shown by chymotrypsin digestion [2, 31 that the N-terminal and C-terminal components of the whole molecule possess amino acid compositions comparable with the same cleaved regions in calf thymus HI [4]. The unusual electrophoretic mobility of P. poljwphalun? HI on gels suggests that the protein has a much higher molecule mass than other HIS; many authors have attempted to determine its molecular mass on this basis [2, 5-81.The histone H1 has been shown to lie in the linker DNA region between nucleosomes [9] with the globular subunit of HI protecting the 168-bp region [lo] and the tails of H1 possibly extending into the core regions of nucleosomes [ll]. The existence of nucleosomes in P. polycephalum is well established [I 21 with the corresponding core particles having between 145 bp [I21 and possibly 154 bp of DNA [13]. Linker lengths of 27 -45 bp between nucleosomes have been reported for Physarum [12,[14][15][16][17].The histone H1 has been shown to be implicated in chromosomal condensation controlled by (a) ionic species and strength [I8 -201; (b) ; (c) phosphorylation during the cell cycle (6, 221.

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The Amino-Acid Sequence of Trout-Testis Histone H1

Cited by 103 publications

References 37 publications

Use of protein blotting to study the DNA‐binding properties of histone H1 and H1 variants

Use of protein blotting to study the DNA‐binding properties of histone H1 and H1 variants

The Primary Structure of Histone H1 from Sperm of the Sea Urchin Parechinus angulosus. 1. Chemical and Enzymatic Fragmentation of the Protein and the Sequence of Amino Acids in the Four N-Terminal Cyanogen Bromide Peptides

Physical studies by NMR and circular dichroism determining three structurally different domains in Physarum polycephalum histone H1

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