Evidence for the close proximity of histones H1 and H3 in chromatin of intact nuclei

Glotov, Boris O.; Itkes, A.V.; Николаев, Л. Г.; Severin, E. S.

doi:10.1016/0014-5793(78)80037-4

Cited by 45 publications

(13 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several properties are shared between histone H 1 and HMG 1: both proteins require linker DNA for stable incorporation into chromatin (Varshavsky et al, 1976;Schroter and Bode. 1982;Nightingale et al, 1996a), they protect linker DNA from nuclease digestion (Simpson, 1978;Nightingale et a!., 1996a), they can have selective interactions with the core histones (Glotov et al, 1978;Boulikas et al, 1980;Bernues et al, 1983), and they both bind four-way junction DNA (Lilley, 1992;Varga-Weisz et al, 1994). Nevertheless, HMG1 and H1 are very different proteins and recognize DNA through distinct mechanisms.…”

Section: Discussionmentioning

confidence: 99%

Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression.

1996

View full text Add to dashboard Cite

Health and Human Development. NIH. Bldg 6. Room Bethesda. MD 2t)892-2710. USA We examined the structural and functional consequences of incorporating either histone HI, histone B4 or HMG1 into a synthetic dinucleosome containing two 5S rRNA genes. We found that all three proteins bind to linker DNA, stabilizing an additional 20 bp from micrococcal nuclease digestion and restrict nucleosome mobility. Histone HI has the highest-affinity interaction with the dinucleosome; histone B4 and HMG1 associate with significantly reduced affinities. We found that histone Hi binds to the dinucleosome template with a dissociation constant (KD) of 7.4 nM, whereas the KD is 45 nM for histone B4 and 300 nM for HMG1. The KDS for the interaction of these proteins with naked DNA are 18 nM for Hi, 80 nM for B4 and 300 nM for HMG1. The differences in association of these proteins with the dinucleosome are reflected in the efficiency with which the different proteins repress transcription from the 5S rRNA genes. Thus, although all three proteins can contribute to the organization of chromatin, the stability of the structures they assemble will vary. Our results provide a molecular explanation for the transcriptional promiscuity of Xenopus early embryonic chromatin, which is enriched in HMG1 and linker histone B4, but deficient in histone Hi.

show abstract

Section: Discussionmentioning

confidence: 99%

Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression.

1996

View full text Add to dashboard Cite

show abstract

“…In addition, HMG1 interacts with both H2A/H2B dimers and (H3/H4)2 tetramers (Bernues et al, 1983). Histone HI can also be cross-linked to H2A and H3 (Glotov et al, 1978;Boulikas et al, 1980). Other similarities include the capacity of both linker histones and HMG1 to form stable complexes with four-way junction DNA (Lilley, 1992;Varga-Weisz etal., 1994).…”

Section: Rkapakpeka Kkkeeededd Deeeddeeed-n R-r-ee Edddde --Gvv-a--s mentioning

confidence: 99%

Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin.

et al. 1996

View full text Add to dashboard Cite

The high mobility group proteins 1 and 2 (HMG1/2) and histone B4 are major components of chromatin within the nuclei assembled during the incubation of Xenopus sperm chromatin in Xenopus egg extract. To investigate their potential structural and functional roles, we have cloned and expressed Xenopus HMG1 and histone B4. Purified histone B4 and HMG1 form stable complexes with nucleosomes including Xenopus 5S DNA. Both proteins associate with linker DNA and stabilize it against digestion with micrococcal nuclease, in a similar manner to histone H1. However, neither histone B4 nor HMG1 influence the DNase I or hydroxyl radical digestion of DNA within the nucleosome core. We suggest that HMG1/2 and histone B4 have a shared structural role in organizing linker DNA in the nucleosome.

show abstract

“…As proposed in reconstitution studies with Hl peptides (11), a direct interaction in native chromatin between tails ofHl and core histone tails could be an attractive possibility to explain our results. Recall that intimate contacts between H3 and Hl (9,10) and between H2A and Hl (65,66) have been demonstrated or strongly suggested. Indications of a possible key role for histone-histone interactions in stabilizing the solenoid come from the surprising observation that limited proteolysis with immobilized proteases is not accompagnied by significant changes in DNA-protein interactions (12).…”

Section: Discussionmentioning

confidence: 94%

“…Moreover, it has also been proposed that core histone tails are involved in the stabilization of higher-order chromatin structure (3,4) and there are some arguments for a fundamental role ofthe N-terminal part ofH3 (5)(6)(7)(8). Intimate contacts between Hl and H3 have been strongly suggested (9,10) and reconstitution and protease digestion studies are consistent with direct interactions between core histone tails and the terminal parts of H 1 (11,12).…”

Section: Introductionmentioning

confidence: 82%

Irreversible Changes Occur in Chromatin Structure Upon Dissociation Of Histone H1

Hacques

Marion²

1990

Journal of Biomolecular Structure and Dynamics

View full text Add to dashboard Cite

The role of histone H1 in the actual interactions bringing about chromatin folding is investigated by studying the reversibility of its dissociation. H1 was dissociated by increase of the NaCl concentration and reassociated by dialysis, without removal from the dialysis bag. To scrutinize the fidelity of this stoichiometric form of chromatin reconstitution, we use circular dichroism, nuclease digestion, thermal denaturation and the sensitive electric birefringence method. No alteration of the repeat length and no nucleosomal sliding are observed upon the reassociation procedure. However, under all the different conditions investigated, the original value of the positive electric birefringence is never recovered, indicating an irreversible change of structure. CD and melting profiles confirm that DNA-protein interactions are modified, and orientational relaxation time measurements indicate that these structural perturbations affect the salt-induced transition of polynucleosomal fibers. The striking conclusion of these studies is that variations of ionic concentration are sufficient to induce irreversible structural alterations affecting the higher-order folding of chromatin. It is of interest that the only sample which exhibits behavior upon reassociation comparable to that of native chromatin is the one which experienced the fastest salt transitions. We suggest that these conformational changes arise from the unbinding to DNA of certain basic tails of histone(s), and that a competition for DNA binding locations exists upon the reassociation. These results are then additional arguments (Mazen, A., Hacques, M.F. and Marion, C.,J. Mol. Biol. 194, 741-745 (1987)), to suggest that dissociation of H1 might modify a direct interaction between basic tails of core histones and H1.

show abstract

Evidence for the close proximity of histones H1 and H3 in chromatin of intact nuclei

Cited by 45 publications

References 12 publications

Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression.

Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression.

Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin.

Irreversible Changes Occur in Chromatin Structure Upon Dissociation Of Histone H1

Contact Info

Product

Resources

About