Thymus-histone

The fluorescence of purified histones has been studied by several different groups, 90 95) with the most detailed studies being on calf thymus histone HI. Histone HI, which binds to the outside of core particles, contains one tyrosine and no tryptophan. This protein exhibits a substantial increase in fluorescence intensity in going from a denatured to a folded state.<90) Collisional quenching studies indicate that the tyrosine of the folded HI is in a buried environ-ment.(91) Libertini and Small(94) have identified three emissions from this residue when in the unfolded state with peaks near 300, 340, and 400 nm. The 340-nm peak was ascribed to tyrosinate (vide infra), and several possibilities were considered for the 400-nm component, including room temperature phosphorescence, emission of a charge transfer complex, or dityrosine. Dityrosine has the appropriate spectral characteristics, but would require... 

Fig. 10. A. Acetic acid-urea-triton-X-100 polyacrylamide gel electrophoresis [15] of the histones used to reconstitute 208-12 nucleosome arrays consisting of recombinant H2A.Z (lane 2) or recombinant H2A.1 (lane 3). Lanes 1 and 4 respectively are chicken erythrocyte and calf thymus histones used as markers [42]. B. Ionic strength (NaCl concentration) dependence of the average sedimentation coelRcient (s2o,w) of reconstituted 208-12 nucleosome arrays containing either H2A.1 (O) or H2A.Z ( ) [42]. The dotted line represents the behavior of a 208-12 complex reconstituted with chicken erythrocyte histones [406]. [Reproduced from Abbott D.W. et al. (2001) I. Biol. Chem. 276, 41945-41949, with permission from The American Society for Biochemistry and Molecular Biology.]...

Paik, W.K and Kim, S. (1973) Enzymatic Demefhylation of Calf Thymus Histones. 

II. Histones, eg., thymus histone. Lota histone, Gadus histone, histone from blood corpuscles. 

The histones contain about 30 per cent, of diamino acids, and only in the case of thymus-histone has an estimation been made of the monoamino acids. They were supposed to be intermediate compounds between protamines and other proteins, and this supposition is confirmed by the results of analysis. 

ATP -I- histone <1, 2, 3> (<1> calf thymus histone II-S, poor substrate... 

S ATP -I- [DNA-directed eukaryotic RNA polymerase II subunit Ila] (<4> distinct from other protein phosphokinases, transfers about 20 phosphates to the heptapeptide repeats Pro-Thr-Ser-Pro-Ser-Tyr-Ser in C-terminal domain of MW 220000 subunit of RNA-polymerase II [7] <4> substrates are RNA-polymerase II subunits of wheat germ, soy bean, pea and human [7] phosphorylates predominantly Ser-residues [1-3,5,7] <1> kinase CTDKl almost exclusively phosphorylates Ser-residues [5] <1> kinase CTDK2 phosphorylates to a lesser extent Thr-resi-dues [1] <3-5> phosphorylates to a lesser extent Thr-residues [1,5,7] <1> phosphorylates Ser- and Thr-residues equally [6] <1,3,5> phosphorylates not Tyr-residues [1,6] <1> kinase CTDKl 33 mol phosphate per mol IIA-subunit [5] <1> kinase CTDK2 40-50 mol phosphate per mol IIA-subunit, i.e. 1 phosphate per heptapeptide repeat [5] <4> no substrate is GTP [7] <2,4> no substrates are CTP and UTP [3,7] <2> no substrates are dTTP and AMP-PNP [3] <4> no substrates are bovine serum albumin and calf thymus histone [7] <5> no substrate is phosvitin... 

Figure 11. Summary of cleavage specificity of deuterolysin from A. oryzae toward calf thymus histone H14.

Other name Aspergillus sojae neutral proteinase II Microbial neutral proteinase II Preferential cleavage of bonds with hydrophobic residues in Pi also Asn3- -Gln and Glys-J.-Ser bonds in insulin B chain. For calf thymus histone H4, high activity towards... 

Figure 3.9. The aromatic region of 270 MHz spectra of caif thymus histone F2A1 in HzO, When NaCl is added aggregation occurs, but only residues 33-101 are involved. The C-2 and C-4 resonances from His 18 therefore remain sharp, whereas those from TyrSl, 72,88,98 and Phe 61 and 100 are broadened out (from [136])...

The e-N-methyllysines have been found in histones (see DeLange and Smith, 1971, 1974), cytochromes c (see DeLange et al. 1970), flagellin (see Glazer et al. 1969), ribosoraal proteins (Comb et al. 1966) and muscle proteins (see Paik and Kim, 1971 for a review). In some proteins (e.g. calf thymus histone III) e-N-monomethyllysine, e-N-dimethyl-lysine and e-N-trimethyllysine are all three present, whereas in other proteins only one derivative (e.g. cytochromes c) or two of the derivatives (e.g. calf thymus histone IV) are present. Methylated lysines can also be formed in proteins by chemical modification in vitro ( 3.1.1.3). 

Calf thymus histone H4 (IV, F2al) is phosphorylated by a specific enzyme on His-18 and His-75. The sequences around these residues are (76) ... 

The amino sequence around the c-N-acetyllysine residues is known in several histones. In calf thymus histone H4 the sequence is (76) ... 

Acetylation occurs near the N-terminal end of the protein and near the sites of methylation (see section on Methylation and Demethylation) of these histones. Residue 16 is the major site of acetylation in both pea and calf thymus histones H4, but other sites may also be acetylated in some cases, particularly residue 8 in pea histone (226) ... 

DeLange et al. (227) suggested that die recognition site for acetylation of calf thymus histones H3 and H4 by one of the acetylation enzymes might be -Lys-X Y-Arg-Lys- Other enzymes with different recognition sites were also indicated by the data. 

Dixon et al. (103) have suggested there are two distinct types of sites for acetylation on histones. Type A site is characterized by an c-N-acetyllysine residue bordered on either side by a small neutral amino acid, while type B site is characterized by an e-N-acetyllysine residue present as a member of Lys-Arg- Arg-Lys, or Lys-Lys pairs. Perhaps two distinct protein (lysine) acetyltransf erases are involved. The sequences around c-N-acetyllysine residues in histones from rainbow trout testis are shown in Table VIII. This hypothesis holds also for the pea and calf thymus histone sequences listed above. 

Dudley KH, Butler TC, Johnson D (1974) Chemical studies of potential relevance to penicillin hypersensitivity kinetic studies of methicillin, phenoxymethylpenicillin and their penicillenic acids. J Pharmacol Exp Ther 188 491-503 Duncan MR, Duncan GR (1973) Binding studies with calf thymus histones and H-cortisol. Can J Pharm Sci 8 115-119... 

Stiittgen G, Masuch E (1973) Exantheme und Hauttestreaktionen auf die Derivate der Pe-nicillansaure Ampicillin und Ciclacillin. Med Klin 68 123-126 Sunaga K, Koide SS (1968) Identification of a prednisolone derivative interacting with calf thymus histones. J Pharm Sci 57 2116-2119... 

Khrapunov, S. N. Protas, A. F. Sivolob, A. V. Dragan, A. I. Berdyshev, G. D. Intrinsic fluorescence, difference spectrophotometry and theoretical-studies on tertiary structure of calf thymus histone-Hl. Int. J. Biochem., 1985, 77(2), 217-222. 

Fig. 2. Effect of various concentrations of sDNA and octadeoxyribonucleotides on rates of polymer formation by poly(ADP-ribose) transferase. NAD+ concentration was 200 xM and 10 xg whole calf thymus histones were added per 0.10 ml incubation mixture. For other det s see Fig. 1 and lef. 8. (Reprinted witii permission from ref. 8).

Poly(ADP-ribosyl)ation at 200 p,M NAD+ as substrate with an excess of whole thymus histones as additional poly(ADP-ribose) acceptors, probably simulating conditions prevailing in chromatin, yielded a less complicated kinetics (Fig. 2). In this system duplex C WAS the best synthetic coenzyme, whereas the activation curve of a sDNA remained sigmoidal. In the cell nucleus, the concentration of DNA is far greater than that of the poly(ADP-ribose) transferase, therefore the observed inhibition in the in vitro model... 

In a remarkable cooperative program between Emil Smith s and James Bonner s laboratories [65, 66], the complete amino acid sequence of the 102 residues of calf thymus histone 4 was established from the chymo-tryptic and tryptic peptides of the purified protein. This study reveals two important characteristics of the histone sequence the presence of an unusual amino acid—acetyllysine—in position 16 and the clustering... 

The amino acid sequence of the T4 histone (glycine, arginine-rich histone) was confirmed in the laboratory of Busch [67] using somewhat different methods of hydrolysis (only one amino acid, arginine in position 44, was found in a different position, namely 40). Of considerable significance with respect to the position of histones in evolution is the fact that the amino acid sequence of the pea seed histone is identical to that of calf thymus histone. 

DeLange, R.J., Fambrough, D.M., Smith, E.L., Bonner, J. Calf and pea histone IV. II. Complete amino acid sequence of calf thymus histone IV. Presence of E-N-acetyllysine. J. biol. Chem. 244, 319-334 (1969)... 

Is the isoelectric point of the protein less than, equal to, or greater than 7 (c) Can a mixture of calf thymus histone and egg albumin be separated by gel electrophoresis with the isoelectric focusing method ... 

Further, Weissman and Graff (621) noted that calf thymus histone also inhibits the respiration of B. anthracis, and that this inhibition is reversed by deoxyribonucleic acid. The concentration of lysine per unit of anthracidal activity is the same for the basic polypeptide and for the histone of thymus. Weissman and Graff (621) hypothesized that the basic polypeptide is a constituent of histone and is liberated from the histone by the acid and heat treatment used for the extraction of the peptide. 

Table 9.1 Characteristics of Calf Thymus Histones and Different Nomenclatures Found In the Literature...

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