On the mechanism of nucleodisome splitting off by nucleases

Поспелов, В. А.; Svetlikova, S. B.

doi:10.1016/0014-5793(82)80725-4

Cited by 10 publications

(5 citation statements)

References 11 publications

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“…35,36 Nucleodisomes cannot be considered as particles per se (as opposed to compact dinucleosomes or altosomes; see below), and must be distinguished from dinucleosomes produced by limited cleavage of linker DNAs in chromatin with micrococcal nuclease. 37 Noteworthy, these dinucleosomes have sometimes been called disomes, and similarly tetranucleosomes and hexanucleosomes were called tetrasomes and hexasomes. 3�� However, oligonucleosomes have a rare occurrence in the literature, perhaps explaining that they abandoned their names to sub-nucleosomal particles (see below).…”

Section: : the Nucleodisomementioning

confidence: 99%

Chromatin Polymorphism and the Nucleosome Superfamily: A Genealogy

Lavelle¹,

Prunell²

2007

Cell Cycle

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Nucleosomes were discovered more than thirty years ago as the basic repeating units of chromatin. Since then, nucleosomes have progressively revealed their taste to come in many appearances, upon either adjunction of other proteins (e.g., a fifth histone or a nonhistone protein, HMG-N), histone substitution for isoforms (histone variants), depletion of one or the two H2A-H2B dimers (sub-nucleosomes), intimate two-particle association, or isomeric structural alterations. The resulting entities, some of them are only transient, acquire new properties useful for their specific roles in chromatin function. These structures are presented here in the chronological order of their identification, from the chromatosome to the sub-nucleosomal hexasome and tetrasome, and from the dinucleosomal altosome and nucleodisome to the nucleosome variants and altered forms: the old lexosome and the most recent reversome.

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Section: : the Nucleodisomementioning

confidence: 99%

Chromatin Polymorphism and the Nucleosome Superfamily: A Genealogy

Lavelle¹,

Prunell²

2007

Cell Cycle

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“…The second criterion for higher order structure that we have employed is the presence of the dinucleosomal periodicity in chromatin as recognized by DNase I (Burgoyne & Skinner, 1982;Klingholz & Stratling, 1982;Pospelov & Svetlikova, 1982). This is a rigorous criterion for higher order structure of the basic higher order 30-nm fiber itself or of a structural state intermediate between the 10-nm filament and the 30-nm fiber (Felsenfeld & McGhee, 1986;Sen et al, 1986;Thoma & Roller, 1981).…”

Section: Discussionmentioning

confidence: 99%

The DNase I sensitive state of "active" globin gene chromatin resists trypsin treatments which disrupt chromatin higher order structure

Lundell¹,

Martinson²

1989

Biochemistry

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Active genes in higher eukaryotes reside in chromosomal domains which are more sensitive to digestion by DNase I than the surrounding inactive chromatin. Although it is widely assumed that some modification of higher order structure is important to the preferential DNase I sensitivity of active chromatin, this has so far not been tested. Here we show that the structural distinction between DNase I sensitive and resistant chromatin is remarkably stable to digestion by trypsin. Chick embryonic red blood cell nuclei were subjected to increasing levels of trypsin digestion and then assayed in the following three ways: (1) by gel electrophoresis for histone cleavage, (2) by sedimentation and nuclease digestion for loss of higher order structure, and (3) by dot-blot hybridization to globin and ovalbumin probes for disappearance of preferential DNase I sensitivity. We have found that chromatin higher order structure is lost concomitantly with the cleavage of histones H1, H5, and H3. In contrast, the preferential sensitivity of the globin domain to DNase I persists until much higher concentrations of trypsin, and indeed is not completely abolished even by the highest levels of trypsin we have used. We therefore conclude that the structural distinction of active chromatin, recognized by DNase I, does not reside at the level of higher order structure.

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“…Nucleic Acids Research ladder extending from one to 10-12 nucleosomes (9). From this is clear that the alteration in chromatin fragmentation cor-relates well with distinct transitions of bu:lk chromatin structure induced by lowering ionic strength.…”

mentioning

confidence: 82%

“…It is known that in such ionic conditions nuclear chromatin is greatly unfolded (17), the linker DNA being very accessible to any nuclease (9,18).…”

Section: Matebi-ai and Methodsmentioning

confidence: 99%

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A structure of potentially active and inactive genes of chicken erythrocyte chromatin upon decondensation

1988

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In the presence of 3 mM MgCl2 DNase I cleavage of bulk, globin and ovalbumin gene chromatin in chicken erythrocyte nuclei generates fragments which are multiples of a double-nucleosome repeat. However, in addition to the dinucleosomal periodicity beta-globin gene chromatin was fragmented into multiples of a 100 b.p. interval which is characteristic for partially unfolded chromatin. This distinction correlates with higher sensitivity of beta-globin domain to DNase I and DNase II as compared to the inactive ovalbumin gene. At 0.7 mM MgCl2 where these DNases fragment bulk chromatin into series of fragments with a 100 b.p. interval, the difference in digestibility of the investigated genes is dramatically decreased. When chromatin has been decondensed by incubation of nuclei in 10 mM Tris-buffer, DNase II generates a typical nucleosomal repeat, and the differential nuclease sensitivity of the analyzed genes is not observed. The data suggest that higher nuclease sensitivity of potentially active genes is due to irregularities in higher order chromatin structure.

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On the mechanism of nucleodisome splitting off by nucleases

Cited by 10 publications

References 11 publications

Chromatin Polymorphism and the Nucleosome Superfamily: A Genealogy

Chromatin Polymorphism and the Nucleosome Superfamily: A Genealogy

The DNase I sensitive state of "active" globin gene chromatin resists trypsin treatments which disrupt chromatin higher order structure

A structure of potentially active and inactive genes of chicken erythrocyte chromatin upon decondensation

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