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Histones, amino acids

Fig. 4. Amino acid sequence of several histone HI proteins to illustrate the macroheterogeneity of linker histones. Amino acid sequence of two highly specialized development-specific members of the histone HI family. A. Oocyte specific mammalian histone Hlfo (previously Hloo) [116]. B. PL-I (EM-1/6) protein from the sperm of the razor clam Ensis minor [120]. These two sequences are shown in comparison to the highly specialized histone H5 from chicken erythrocytes. The regions corresponding to the trypsin-resistant (winged helix motif [96]) which is characteristic of the protein members of the histone HI family are indicated by a box and have been aligned to show the sequence similarity. Fig. 4. Amino acid sequence of several histone HI proteins to illustrate the macroheterogeneity of linker histones. Amino acid sequence of two highly specialized development-specific members of the histone HI family. A. Oocyte specific mammalian histone Hlfo (previously Hloo) [116]. B. PL-I (EM-1/6) protein from the sperm of the razor clam Ensis minor [120]. These two sequences are shown in comparison to the highly specialized histone H5 from chicken erythrocytes. The regions corresponding to the trypsin-resistant (winged helix motif [96]) which is characteristic of the protein members of the histone HI family are indicated by a box and have been aligned to show the sequence similarity.
Charge neutralization. Given the histone amino acid sequences illustrated below, estimate the charge of a histone octamer at pH... [Pg.920]

M.p. 207°C. The naturally occurring substance is dextrorotatory. Arginine is one of the essential amino-acids and one of the most widely distributed products of protein hydrolysis. It is obtained in particularly high concentration from proteins belonging to the prolamine and histone classes. It plays an important role in the production of urea as an excretory product. [Pg.41]

CfiHqNaO . M.p. 277 C. The naturally occurring substance is laevorotatory. Histidine is one of the basic amino-acids occurring in the hydrolysis products of proteins, and particularly of the basic proteins, the protamines and histones. It is an essential constituent of the food of animals. [Pg.205]

H2N-CH2 [CH2j3.CH(NH2) COOH. Colourless needles, m.p. 224 C (decomp.), very soluble in water, insoluble in alcohol. L-(-H)-Lysine is one of the basic amino-acids occurring in particularly large quantities in the protamine and histone classes of proteins. It is an essential amino-acid, which cannot be synthesized by the body and must be present in the food for proper growth. It can be manufactured by various fermentation processes or by synthesis. [Pg.244]

Histone H3 Histones are DNA-binding proteins found in chromosomes 135 amino acid residues. Note die very basic nature of this protein dne to its abmidance of Arg and Lys residues. It also lacks tryptophan. [Pg.114]

Histone proteins share distinct features including a high content of basic amino acids, lysines and arginines,... [Pg.592]

The similarity of the various histone fibers is probably correlated with the similarity in the distribution of the amino acids in the sequences of the four core histones and reflects their function as the skeleton or backbone of chromatin. However, from the presence of a specific pattern of interactions of the core histones and the existence of histone variants and histone postsynthetic modifications, one can anticipate modulations in the basic general pattern of histone structure. In Section V, a possible mechanism for histone microheterogeneity influencing chromatin structure is suggested. Analogous to other assembly systems, small subunit modifications may be amplified to produce major changes in the assembled superstructure. [Pg.3]

Fic. 1. The amino acid sequences of calf histones H2A (Yeoman et al., 1972 Sau-tiere et al., 1974) and H2B (Iwai et al., 1972). A one-letter code is used A, alanine R, arginine N, asparagine D, aspartic acid C, cysteine E, glutamic acid Q, glutamine ... [Pg.6]

Fig. 2. The amino acid sequencies of calf histone H4 (DeLange et al., 1972 Ogawa et al, 1969) and H3 (DeLange et al., 1972 Olson et al., 1972 DeLange et al., 1973). The notation is as in Fig. 1 except that superscript M denotes methylation site. Fig. 2. The amino acid sequencies of calf histone H4 (DeLange et al., 1972 Ogawa et al, 1969) and H3 (DeLange et al., 1972 Olson et al., 1972 DeLange et al., 1973). The notation is as in Fig. 1 except that superscript M denotes methylation site.
This mode of binding of HI to the nucleosome is consistent with the findings that at low histone-to-DNA ratios and/or at low ionic strength histone HI binds preferentially to supercoiled DNA (Vogel and Singer, 1975, 1976). This preferential binding has been shown to be the property of the HI peptide fragment, amino acid residues (73-106). [Pg.33]

Figure 1. Hierarchical model of chromosome structure, (a) In interphase cells, DNA is packed in a nucleus as forming nucleosome and chromatin, (b) DNA forms nucleosome structure together with core histone octamer, which is then folded up into 30nm fiber with a help of linker histone HI. This 30 nm fiber is further folded into 80 nm fiber and 300 nm loop structures in a nucleus. In mitosis, chromosome is highly condensed. Proteins which are involved in each folding step are indicated above and non-protein factors are indicated below, (c) The amino acid sequences of histone tails (H2A, H2B, H3 and H4) are shown to indicate acetylation, methylation and phosphorylation sites. (See Colour Plate 1.)... Figure 1. Hierarchical model of chromosome structure, (a) In interphase cells, DNA is packed in a nucleus as forming nucleosome and chromatin, (b) DNA forms nucleosome structure together with core histone octamer, which is then folded up into 30nm fiber with a help of linker histone HI. This 30 nm fiber is further folded into 80 nm fiber and 300 nm loop structures in a nucleus. In mitosis, chromosome is highly condensed. Proteins which are involved in each folding step are indicated above and non-protein factors are indicated below, (c) The amino acid sequences of histone tails (H2A, H2B, H3 and H4) are shown to indicate acetylation, methylation and phosphorylation sites. (See Colour Plate 1.)...
Linker histones (HI, H5 and others) are also major components of metaphase chromosome, and occupy 5.8% of the total protein amount (Uchiyama et al, 2005). They play an important role in the formation of the 30 nm fiber (see also section 2.3). These linker histones carry more lysine residues ( 30% of the total amino acids) than the core histones and have a core domain in the middle part that binds to a nucleosome. The linker histones could be easily extracted from the chromatin with 0.5 M NaCl, whereas the core histone octamers need more than 0.8 M NaCl to dissociate from nucleosomes. [Pg.9]

Figure 1. Variants of the histones H3 from yeast Saccharomyces cerevisiae S.c.), fruit fly Drosophila melanogaster D.m), and human Homo sapiens H.s.). H3.1 is identical to H3.2 with the exception of a serine to cysteine exchange (top). H3.3 differs from H3.1/H3.2 only in four amino acid positions. Centromer-specific histones (CenH3 s) have an amino terminus of variable length (between 20 and 200 residues). They also possess an extended loop 1 region in the histone fold domain... Figure 1. Variants of the histones H3 from yeast Saccharomyces cerevisiae S.c.), fruit fly Drosophila melanogaster D.m), and human Homo sapiens H.s.). H3.1 is identical to H3.2 with the exception of a serine to cysteine exchange (top). H3.3 differs from H3.1/H3.2 only in four amino acid positions. Centromer-specific histones (CenH3 s) have an amino terminus of variable length (between 20 and 200 residues). They also possess an extended loop 1 region in the histone fold domain...
H2A Barr body-deficient (Bbd) is an evolutionary relatively young histone variant sharing only about 48% amino acid sequence similarity to H2A. This histone variant appears to be specific for mammals (Chadwick and Willard 2001). As indicated by the name, the transcriptionally inactive and highly condensed X chromosome in female mammals (also known as Barr body ) is depleted for H2A , while this variant is detectable in autosomes and the active sex chromosomes. This observation suggested that H2A is linked to transcriptionally active euchromatin. H2A cofractionates in sedimentation centrifugation with hyper-acetylated histone H4, further corroborating that it associates with transcriptionally active euchromatin. [Pg.102]


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See also in sourсe #XX -- [ Pg.231 , Pg.233 ]




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