Involvement of the globular domain of histone H1 in the higher order structures of chromatin

Losa, Riccardo; Thoma, Fritz; Koller, Th.

doi:10.1016/0022-2836(84)90183-9

Cited by 67 publications

(20 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1 b, e, and k). The stem motif is consistent with work demonstrating that the structured central domain of the linker histones binds near the linker DNA entry-exit region of the nucleosome (43,44), and both the central and C-terminal domains are required for normal chromatin folding (26,45). However, the precise locations of these histone domains within the stem structure remain to be determined.…”

Section: Resultssupporting

confidence: 69%

Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin

Bednář

Horowitz

Grigoryev

et al. 1998

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

536

496

View full text Add to dashboard Cite

The compaction level of arrays of nucleosomes may be understood in terms of the balance between the selfrepulsion of DNA (principally linker DNA) and countering factors including the ionic strength and composition of the medium, the highly basic N termini of the core histones, and linker histones. However, the structural principles that come into play during the transition from a loose chain of nucleosomes to a compact 30-nm chromatin fiber have been difficult to establish, and the arrangement of nucleosomes and linker DNA in condensed chromatin fibers has never been fully resolved. Based on images of the solution conformation of native chromatin and fully defined chromatin arrays obtained by electron cryomicroscopy, we report a linker histone-dependent architectural motif beyond the level of the nucleosome core particle that takes the form of a stem-like organization of the entering and exiting linker DNA segments. DNA completes Ϸ1.7 turns on the histone octamer in the presence and absence of linker histone. When linker histone is present, the two linker DNA segments become juxtaposed Ϸ8 nm from the nucleosome center and remain apposed for 3-5 nm before diverging. We propose that this stem motif directs the arrangement of nucleosomes and linker DNA within the chromatin fiber, establishing a unique threedimensional zigzag folding pattern that is conserved during compaction. Such an arrangement with peripherally arranged nucleosomes and internal linker DNA segments is fully consistent with observations in intact nuclei and also allows dramatic changes in compaction level to occur without a concomitant change in topology.

show abstract

Section: Resultssupporting

confidence: 69%

Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin

Bednář

Horowitz

Grigoryev

et al. 1998

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

536

496

View full text Add to dashboard Cite

show abstract

“…Total avian histones were used as size standards (Fig. 3A, S), since the C-terminal cleavage products are known to migrate between H1 and the core histones (64). [ 35 S]BAF bound fulllength linker histones and C-tail fragments (Fig.…”

Section: Resultsmentioning

confidence: 99%

Binding of Barrier to Autointegration Factor (BAF) to Histone H3 and Selected Linker Histones Including H1.1

Lee

Wilson

2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

Barrier to autointegration factor (BAF) is an essential conserved double-stranded DNA-binding protein in metazoans. BAF binds directly to LEM domain nuclear proteins (e.g. LAP2, Emerin, and MAN1), lamin A, homeodomain transcription factors, and human immunodeficiency virus type 1-encoded proteins. BAF influences higher order chromatin structure and is required to assemble nuclei. BAF also facilitates retroviral preintegration complex insertion into target DNA in vitro, through unknown mechanisms. We report that BAF binds directly and selectively to linker histone H1.1 (among three subtypes tested) and core histone H3 with affinities of ϳ700 nM and ϳ100 -200 nM, respectively, in vitro and in vivo. Mutations at the bottom and top surfaces of the BAF dimer disrupted or enhanced, respectively, this binding and affected H1 and H3 similarly. Biochemical studies showed that C-terminal residues 108 -215 of histone H1.1 and the N-terminal tail plus helix ␣N in the core of histone H3.1 were each necessary and sufficient to bind BAF. Based on its interactions with histones and DNA, we propose BAF might bind nucleosomes in vivo.

show abstract

“…The structural and functional roles of the individual domains of Hi are less clear. The globular region appears to be sufficient for sealing the nucleosome in vitro (1) and was suggested to organize the 30-nm fibers (33,58). The Nterminal tail and, in particular, the positively charged Cterminal tail might bind to linker DNA or adjacent nucleosomes and thereby contribute to the condensation of chromatin fibers (27,58 …”

mentioning

confidence: 99%

Histone H1 expressed in Saccharomyces cerevisiae binds to chromatin and affects survival, growth, transcription, and plasmid stability but does not change nucleosomal spacing.

Linder¹,

Thoma²

1994

Mol. Cell. Biol.

View full text Add to dashboard Cite

Histone HI is proposed to serve a structural role in nucleosomes and chromatin fibers, to affect the spacing of nucleosomes, and to act as a general repressor of transcription. To test these hypotheses, a gene coding for a sea urchin histone Hi was expressed from the inducible GAL] promoter in Saccharomyces cerevisiae by use of a YEp vector for high expression levels (strain YCL7) and a centromere vector for low expression levels (strain YCL1). The Hi protein was identified by its inducibility in galactose, its apparent molecular weight, and its solubility in 5% perchloric acid. When YCL7 was shifted from glucose to galactose for more than 40 h to achieve maximal levels of HI, Hi could be copurified in approximately stoichiometric amounts with core histones of Nonidet P-40-washed nuclei and with soluble chromatin fractionated on sucrose gradients. While S. cerevisiae tolerated the expression of low levels of Hi in YCLI without an obvious phenotype, the expression of high levels of HI correlated with greatly reduced survival, inhibition of growth, and increased plasmid loss but no obvious change in the nucleosomal repeat length. After an initial induction, RNA levels for GALi and Hi were drastically reduced, suggesting that Hi acts by the repression of galactose-induced genes. Similar effects, but to a lower extent, were observed when the C-terminal tail of HI was expressed.Most of the eukaryotic genome is packaged by histone proteins into nucleosomes, 30-nm chromatin fibers, and higher-order structures. The Hi class of histones includes a variety of subtypes or variants of lysine-rich proteins with a short N-terminal tail, a central globular domain, and a long, highly charged C-terminal tail. Hi is proposed to serve different roles (for a review, see reference 62). (i) At the nucleosome level, DNA is wrapped in two superhelical turns around an octamer of core histones (two each of H2A, H2B, H3, and H4). Our current view is that on the average, one histone HI molecule binds from the outside at the entry and exit site of the linker DNA and stabilizes two turns of DNA in the nucleosome. This view is supported by electron microscopy (16, 57), proteinprotein cross-linking (8) (4,37,58). The structural and functional roles of the individual domains of Hi are less clear. The globular region appears to be sufficient for sealing the nucleosome in vitro (1) and was suggested to organize the 30-nm fibers (33,58). The Nterminal tail and, in particular, the positively charged Cterminal tail might bind to linker DNA or adjacent nucleosomes and thereby contribute to the condensation of chromatin fibers (27,58

show abstract

Involvement of the globular domain of histone H1 in the higher order structures of chromatin

Cited by 67 publications

References 52 publications

Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin

Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin

Binding of Barrier to Autointegration Factor (BAF) to Histone H3 and Selected Linker Histones Including H1.1

Histone H1 expressed in Saccharomyces cerevisiae binds to chromatin and affects survival, growth, transcription, and plasmid stability but does not change nucleosomal spacing.

Contact Info

Product

Resources

About