Interaction of histones H1 and H1° with superhelical and linear DNA

Yaneva, Julia; Zlatanova, Jordanka; Paneva, Elena; Srebreva, Ljuba; Tsanev, Roumen

doi:10.1016/0014-5793(90)81379-3

Cited by 14 publications

(3 citation statements)

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“…6). While direct competition experiments confirmed the claimed preference for superhelical DNA molecules in the case of Hi (11,12) and H10 (12), the issue of whether histone H5 [the Hi variant specific to nucleated erythrocytes (13, 14)] possesses such a property is still a matter of controversy (11,15).Previous studies of this phenomenon are subject to a general criticism. In most cases plasmid or viral DNA preparations were used that were poorly characterized with respect to their topological state.…”

mentioning

confidence: 81%

Histones H1 and H5 interact preferentially with crossovers of double-helical DNA.

Krylov

Leuba

Holde

et al. 1993

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

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The interaction of the linker histones Hl and H5 from chicken erythrocyte chromatin with pBR322 was studied as a function of the number of superhelical turns in circular plasmid molecules. Supercoiled plasmid DNA was relaxed with topoisomerase I so that a population with a narrow distribution of topoisomers, containing from zero to five superhelical turns, was obtained. None of the topoisomers contained alternative non-B-DNA structures. Histone-DNA complexes formed at either 25 or 100 mM NaCI fmal concentration and at histone-DNA molar ratios ranging from 10 to 150 were analyzed by agarose gel electrophoresis. The patterns of disappearance of individual topoisomer bands from the gel were interpreted as an indication of preference of the linker histones for crossovers of double-helical DNA. This preference was observed at both salt concentrations, being more pronounced under conditions of low ionic strength. Isolated H5 globular domain also caused selective disappearance of topoisomers from the gel, but it did so only at very high peptide-DNA molar ratios. The observed preference of the linker histones for crossovers of double-helical DNA is viewed as a part of the mechanism involved in the sealing of the two turns of DNA around the histone octamer.The lysine-rich histones (Hi and its variants) interact with the linker DNA between nucleosomes, sealing two turns of DNA around the nucleosome core (1). They are also involved in forming higher-order structures of the chromatin fiber (for reviews, see refs. 2 and 3). Recent evidence shows that the lysine-rich histones are involved in the regulation of gene transcription (reviewed in refs. 4-7).One of the main features of the interaction of Hi and DNA is the preference of this histone for superhelical DNA. However, the original work from Singer's laboratory (8-10), which indicated that Hi had a higher affinity for superhelical than for relaxed circular or linear DNA, has been questioned on a number of occasions (see ref. 6). While direct competition experiments confirmed the claimed preference for superhelical DNA molecules in the case of Hi (11,12) and H10 (12), the issue of whether histone H5 [the Hi variant specific to nucleated erythrocytes (13, 14)] possesses such a property is still a matter of controversy (11,15).Previous studies of this phenomenon are subject to a general criticism. In most cases plasmid or viral DNA preparations were used that were poorly characterized with respect to their topological state. Either total populations of closed circular DNA were used directly as isolated from bacterial or eukaryotic cells or high levels of supercoiling were induced by incubating nicked circular molecules with ethidium bromide and then ligating or treating with topoisomerase in the presence of the intercalator. In such preparations the superhelical density is not precisely known, and it isThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U...

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mentioning

confidence: 81%

Histones H1 and H5 interact preferentially with crossovers of double-helical DNA.

Krylov

Leuba

Holde

et al. 1993

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

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“…Electrophoresis (De Bernardin et al, 1986), sedimentation (Bottger et al, 1976(Bottger et al, , 1981Singer and Singer, 1978;D'Anna et al, 1979;Vogel and Singer, 1975a), and filter-binding experiments Singer, 1975a,b, 1976;Yaneva et al, 1990) have demonstrated a preferential interaction of HI with superhelical DNA and suggested that the extent of interaction may be related to the degree of superhelicity. Moreover, a biphasic response of HI binding to titration with ethidium bromide (EthBr) was observed in sedimentation (Bottger et al, 1981;Vogel and Singer, 1975b) and filter-binding experiments (Vogel and Singer, 1975b), suggesting that HI binds preferentially to both negatively and positively supercoiled DNA, as compared to the relaxed form.…”

Section: Introductionmentioning

confidence: 99%

Histone H1 preferentially binds to superhelical DNA molecules of higher compaction

Ivanchenko

Zlatanova

Holde

1997

Biophysical Journal

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In chromatin, the physiological amount of H1 is one molecule per nucleosome or, roughly, one molecule per 200 bp of DNA. We observed that at such a stoichiometry, H1 selectively binds to supercoiled DNA with magnitude of sigma > or = 0.012 (both negative and positive), leaving relaxed, linear, or nicked DNA molecules unbound. When negative and positive DNA topoisomers of varying superhelicity are simultaneously present in the binding mixture, H1 selectively binds to the molecules with highest superhelicity; less supercoiled forms are gradually involved in binding upon increasing the amount of input protein. We explain this topological preference of H1 as the consequence of an increased probability for more than one H1-DNA contact provided by the supercoiling. The existence of simultaneous contacts of H1 with both intertwined DNA strands in the supercoiled DNA molecules is also inferred by topoisomerase relaxation of H1-DNA complexes that had been prefixed with glutaraldehyde.

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“…Formation of histone H1/DNA complexes and drugcompetition assay the complexes of linker histones h1, h5 and GD5 with each of the DnA-fragments (large or small, ActD-treated or intact) were created by direct mixing with 1µg DnA in 15 µl sample mixture containing 20 mM tris-hcl, ph 7.5, 20 mM nacl, 0.1 mM eDtA, 0.1mM phenylmethylsulfonyl fluoride (PMSF), at protein to DNA ratio of 1.0 w/w (15,16,17). Following incubation for 25 min at room temperature (usually 23 o c), 1.5 µl of a loading mix (0.1 % bromophenolblue, 30 % glycerol) was added and the samples electrophoresed on 1.0% agarose gel for the large DnA-fragment and on 15 % polyacrylamide gel (29:1 AA to bisAA) for the small 34 bp fragment.…”

Section: Antibiotic Solutions and Drug Treatment Of Dnamentioning

confidence: 99%