Chemical crosslinking of histone H1° to histone neighbours in nuclei and chromatin

Dashkevich, Viktor K.; Николаев, Л. Г.; Zlatanova, Jordanka; Glotov, Boris O.; Severin, E. S.

doi:10.1016/0014-5793(83)80594-8

Cited by 8 publications

(2 citation statements)

References 26 publications

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“…The existence of possible interaction between HI0 and other Hi fractions (17,18,19) which are not present in the reconstituted samples, made with only one pure histone fraction, may be the basis for further investigation. On the other hand, supranucleosomal structures, as described recently (20), involving Hi linking of adjacent nucleosomes, may have different properties depending on which histone fraction is concerned.…”

Section: Discussionmentioning

confidence: 99%

The involvement of histone H1° in chromatin structure

et al. 1985

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Micrococcal nuclease digestion and light scattering are used to compare native chromatins with various histone H10 contents. The experimental data show that the higher the Hi0 content, the greater the ability to form compact structures with increasing ionic strength, and the lower the DNA accessibility to micrococcal nuclease. On the contrary, reconstituted samples from HI-depleted chromatin and pure individual HI fractions behave in such a way that samples reconstituted with pure H10 give rise to a looser structure, more accessible to nuclease than samples reconstituted with Hi-1. This contradiction suggests that the effect of Hi0 on chromatin structure must originate from the interaction of this histone with other components in native chromatin among which other histone HI subfractions are good candidates. INTRODUJCTIONH10, a histone of the HI family, is regulated during development (1,2) and it has been suggested that HI0 could be implicated in cellular differenciation (2).Like Hi, H10 is located on the linker region of the nucleosome (1). We have found, as previously reported, that H10 is associated with an increased resistance of chromatin to micrococcal nuclease digestion (3). This result suggested that HI0 could be associated with, or responsible for, a more compact conformation of chromatin. In the present report, we have studied chromatin samples from newborn mouse liver, adult rat liver and adult mouse liver having respectively 3%, 7% and 21% of HI0 relative to total Hi. We have compared their resistance to micrococcal nuclease, and their ability to condense by a light scattering study (4, Girardet J.L. and Roche J., in preparation). We found an increased resistance to the nuclease associated with a greater amount of HIQ. Light scattering studies showed that the greater the amount of HI0, the easier the chromatin can take up compact conformation with increasing ionic strength.

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Section: Discussionmentioning

confidence: 99%

The involvement of histone H1° in chromatin structure

et al. 1985

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“…The histone genes present in greatest abundance appear to be active in early development when there is a great demand for new histone synthesis, whereas the minor variants are made at later stages of development and represent the major histones present in somatic cells. The genes for these variant histones may or may not be associated with the tandemly repeated blocks [105][106][107][108][109][110] (section 9.2).…”

Section: Histones and Non-histone Proteins (A) Histonesmentioning

confidence: 99%

Genomes of eukaryotes, bacteria and viruses: chromosome organization

Adams

Knowler

Leader

1992

The Biochemistry of the Nucleic Acids

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The function of DNA is to carry the genetic message from generation to generation, and to allow the expression of that message under appropriate conditions. DNA molecules are very large and carry the information for the synthesis of many proteins, not all of which are required at the same time. Problems will obviously arise when it comes to packaging such long lengths of DNA into a cell in such a way as to allow programmed access to the encoded information. These problems are compounded by the fact that R. L. P. Adams et al., The Biochemistry of the Nucleic Acids

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