Interactions of histone LAK (f2a2) with histones KAS (f2b) and GRK (f2a1)

D'Anna, Joseph A.; Isenberg, Irvin

doi:10.1021/bi00707a016

Cited by 100 publications

(49 citation statements)

References 32 publications

(14 reference statements)

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“…This is consistent with the fact that isolated histones can interact with each other in a very defined and often complex manner (9)(10)(11)(12).…”

Section: Nh2supporting

confidence: 86%

Release of discrete subunits after nuclease and trypsin digestion of chromatin.

Weintraub¹

1975

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

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Digestion of chromatin with DNase (nucleate 3'-oligonucleotidohydrolase, EC 3.1.4.7) releases 11-12S nucleoprotein particles. After extensive nuclease digestion, the DNA in these particles consists of a collection of eight discrete DNA fragments. When these nuclease-particles are treated with trypsin (EC 3.4.21.4), only 20 to 30 amino-acid residues are cleaved from histone Nterminals, the histone C-terminal segments being resistant. The resulting 5S nucleoprotein particles have now been shown on acrylamide gels to consist of a series of eight discrete DNA-containing bands. Four of these bands contain C-terminal cleavage fragments from four histones (III, IV, Ib2, and Ilbi) tightly bound to them; a fifth contains fragments from only histones III and IV. The remaining three bands contain only DNA. Since these protein-free DNA bands were resistant to nuclease prior to trypsin treatment, they were presumably associated with histone N-terminal segments in the native structure.Trypsin, therefore, appears to split nuclease-particlps, releasing two subfractions of DNA-one associated with protein, the other not. The data is compatible with a model in which the majority of DNA in the eukaryotic nucleus is folded into hairpin loops of double-stranded helix, each created by the concerted cross-linking action of 6 to 10 histones which interact to form a trypsin-resistant complex composed, for the most part, of all four major histones. These loops may further fold upon themselves to form the "nu" bodies that have been visualized by electron microscopy.The DNA in chromatin is digested by staphylococcal nuclease (nucleate 3'-oligonucleotidohydrolase, EC 3.1.4.7) into eight discrete, limit-digest DNA fragments (1, 2), which range in size between 45 and 145 base pairs. Yet, partial staphylococcal nuclease digestion results in the appearance of transient DNA fragments of 200 base pairs or integer multiples of that size (3,4). A reasonable interpretation of these findings is that these larger transient segments are generated by a regular arrangement of very accessible, DNase-sensitive sites, while the eight bands of the limit-digest are generated by the further digestion of less accessible but discrete sites within each 200-base-pair repeat. Recent electron microscope data has shown that "bead-like" structures occur at regular intervals of about 200 base pairs along the extended chromosome fiber (5). It is thus tempting to consider that the initial nuclease cut is between these so-called "nu" bodies (5), and that further digestion introduces a limited number of specific cuts within each "nu" body.Exhaustive treatment of chick erythrocyte chromatin with trypsin (EC 3.4.21.4) results in the complete digestion of histones I and V and the cleavage of only 20 to 30 amino-acid residues from the positively charged N-terminal parts of histones III, IV, IIb2, and (possibly) IHbl (2). In this comAbbreviations: ST, produced by treatment with staphylococcal nuclease followed by trypsin; TS, trypsin followed by nuclease. munication I...

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“…This is consistent with the fact that isolated histones can interact with each other in a very defined and often complex manner (9)(10)(11)(12).…”

Section: Nh2supporting

confidence: 86%

Release of discrete subunits after nuclease and trypsin digestion of chromatin.

Weintraub¹

1975

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

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“…An increase in the helix content has frequently been correlated with the induction of specific crossinteractions between the histones (cf. [40]). Our results would hence support a model in which the interhistone contacts are strengthened due to an extension of a-helical sections.…”

Section: Circular Dichroismmentioning

confidence: 99%

Modulation of the Nucleosome Structure by Histone Acetylation

Bode

Henco

Wingender

1980

European Journal of Biochemistry

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A rapid procedure for the isolation of core particles from Chinese hamster ovary cells is described which permits measurements, usually at the day of their preparation. Particles of 145 f 5 base pairs, derived from interphase cells, will be compared with the analogue specimens from butyrate-treated cells, metaphase cells and a standard preparation from chicken erythrocytes. Butyrate cause an increase in the acetylation of histones H3 and H4, which induces alterations of the interhistone and histone-DNA interactions. Changes in the interhistone contacts, correlated to an extension of a-helical segments, lead to an altered accessibility of the H3 cysteine side-chains and to a different histone displacement by protamines. On the other hand, histone-DNA contacts are loosened in parts and this is particularly evident from the changes in the premelting region of a thermaldenaturation profile.In the structural element of chromatin two each of histones H2a, H2b, H3 and H4 form an octameric protein core which is surrounded by a 140-base-pair segment of DNA. These 'core particles' are linked by a variable segment of DNA to reveal a repeating subunit structure (nucleosome) [l]. Specific lysine side-chains within the highly basic aminoterminal regions of histone H3 (residues 9, 14, 18 and 23) and histone H4 (residues 5, 8, 12 and 16)

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“…Kornberg and Thomas (6) suggested that the protein core consisted of two each of four histones (H2a, H2b, H3, and H4) on the basis of crosslinking experiments and x-ray patterns. D'Anna and Isenberg (7) demonstrated that the histones bind to each other as specific pairs in solution with the tightest binding between H3 and H4. These two formed a tetramer (i.e., homotypic) to which two molecules each of H2a and H2b bound less tightly.…”

mentioning

confidence: 99%

Chromatin structure in the cellular slime mold Dictyostelium discoideum.

Bakke¹,

Wu²,

Bonner³

1978

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

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The structure of Dictyosteium discoideum chromatin has been studied by the following techniques: electron microscopy, staphylococcal nuclease digestion, acrylamide gel electrophoresis, sucrose gradient centrifugation, and melting. The basic unit of chromatin is the nucleosome, which is a particle 98.6 A in diameter. Approximately 50% of the chromatin is protected from nuclease digestion, but this decreases when protease activity is not inhibited. The nucleosome contains 187 base pairs of DNA, including a 137-base-pair core and a 50-base-pair linker. The monomer nucleosome has an ssow value of 11.5 S on isokinetic sucrose gradients. When the chromatin is melted, four transitions are observed, at 54.5°, 6.7', 74.90, and 79.70. The structure of Dictyostelium chromatin is very similar to that seen in higher eukaryotes.Olins and Olins (1) The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. 705produces a stable core length of DNA, which is about 140 bp in all organisms that have been investigated. The DNA between the cores is the linker and is covered by either HI or its equivalent (14). Histones more basic than HI, such as H5, may require longer linkers.Lower eukaryotes, such as Detyostelium discoideum, are well suited for studying chromatin structure and gene expression. Because the slime mold has a large fraction of templateactive chromatin, any structural differences in the active and inactive chromatin should be observable. One aspect of chromatin structure is confirmed in the following study. Dietyostelium has a less basic histone HI than higher eukaryotes and also has a shorter length of linker DNA in the nucleosome. In addition, the presence of four, instead of the usual five, histones does not affect the basic chromatin structure. METHODSGrowth and Labeling of Cells. A variant of Dictyostelium dideum (Ax 3) is grown in an axenic culture (15) on a rotary shaker. The DNA is labeled with [3H]thymidine for the nuclease digestion studies. The cells are first grown to 1 X 107 cells per ml. They are harvested and washed by centrifugation. They are then suspended at 1 X 108 cells per ml in 20 mM KCI/2.5 mM MgCl2/50 mM sodium phosphate buffer, pH 6.5/[3H]-thymidine at 4 ,Ci/ml and shaken for 8 hr. At the end of this time they are transferred to a minimal growth medium containing, per liter, 10 g of glucose, 10 g of proteose peptone (Difco), 0.5 g of yeast extract, 5 mM phosphate buffer at pH 6.6, 0.02 mg of biotin, 0.005 mg of cyanocobalamine, 0.2 mg of folic acid, 0.4 mg of lipoic acid, 0.5 mg of riboflavin, and 0.5 mg of thiamine (16)

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Interactions of histone LAK (f2a2) with histones KAS (f2b) and GRK (f2a1)

Cited by 100 publications

References 32 publications

Release of discrete subunits after nuclease and trypsin digestion of chromatin.

Release of discrete subunits after nuclease and trypsin digestion of chromatin.

Modulation of the Nucleosome Structure by Histone Acetylation

Chromatin structure in the cellular slime mold Dictyostelium discoideum.

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