Histone H1

DEVELOPMENTAL BIOLOGY

Embryonic

The first appearance of H1 takes place during cycles 7 and 8. It is during cycle 7 that the size of the nuclei begins to decrease. By cycles 10-12 a sufficient amount of H1 has accumulated to allow the reorganization of chromatin to a transcriptionally active state. Subsequently, increased zygotic transcription elevates H1 levels even further. This exponential increase, together with the increased number of nuclei, rapidly depletes the relative levels of HMG-D protein. It has been suggested that the chromatin generated in the presence of HMG-D is transcriptionally silent, and that transcription begins only when H1 levels have reached a particular threshold value and overcome the HMG-D effects, around nuclear cycle 10 (Ner, 1994).

The amount of histone H1 relative to core histones (See Histone H4) has been determined in three Drosophila species (D. melanogaster, D. texana and D. virilis) in chromatin from several tissues differing in chromatin structure and genetic activity. Low levels of H1 are found in relatively undifferentiated, early embryos as well as in a line of cultured cells. In late embryos the content of H1 is highest in D. virilis, which possesses larger amounts of and a partially more compacted constitutive heterochromatin than the two other species. Polytene chromatin from larval salivary glands shows increased levels of H1 compared with diploid chromatin; the degree of phosphorylation of this histone is relatively low. The degree of phosphorylation of H2A is found to be drastically reduced in polytene as compared with diploid embryonic chromatin, which parallels the extensive underreplication of constitutive heterochromatin. In diploid chromatin, a qualitative correlation is also observed between the relative amounts of heterochromatin and the levels of H2A phosphorylation. These findings suggest a connection between H2A phosphorylation and heavy compaction of interphase chromatin (Holmgren, 1985).

HMG-D is an abundant chromosomal protein associated with condensed chromatin during the first nuclear cleavage cycles of the developing Drosophila embryo. It previously suggested that HMG-D might substitute for the linker histone H1 in the preblastoderm embryo and that this substitution might result in the characteristic less compacted chromatin. The association of HMG-D with chromatin has been studied using a cell-free system for chromatin reconstitution derived from Drosophila embryos. Association of HMG-D with chromatin, like that of histone H1, increases the nucleosome spacing indicative of binding to the linker DNA between nucleosomes. HMG-D interacts with DNA during the early phases of nucleosome assembly but is gradually displaced as chromatin matures. By contrast, purified chromatin can be loaded with stoichiometric amounts of HMG-D, and this can be displaced upon addition of histone H1. A direct physical interaction between HMG-D and histone H1 was observed in a Far Western analysis. The competitive nature of this interaction is reminiscent of the apparent replacement of HMG-D by H1 during mid-blastula transition. These data are consistent with the hypothesis that HMG-D functions as a specialized linker protein prior to appearance of histone H1 (Ner, 2001).

Histone H1 and HMGB1 proteins could influence chromatin structure in a similar manner by binding to linker DNA sequence. Histone H1 associates with linker DNA sequences and organizes nucleosomal arrays into higher order chromatin structures, such as the 30-nm chromatin fiber. However, little is known about how HMGB1 interacts with the nucleosome and about the consequences in structure and function. H1 and HMGB1 share important features; both protect linker DNA sequences from nuclease digestion, and both bind four-way junctions. Consistent with the idea that interaction of HMGB1 might replace histone H1, in the very early stages of Drosophila embryogenesis histone H1 is absent, but the high mobility group protein D (HMG-D) is present in vast excess. Based on the similarities between HMG-D and H1, a role for HMG-D as a linker protein compatible with and perhaps required for the fast condensation-decondensation cycles associated with the very rapid nuclear division cycles found in preblastoderm embryos has been suggested. An analogous role has been proposed for the Xenopus HMGB1 and B4 proteins; both proteins have been demonstrated to bind di-nucleosomal DNA (Ner, 2001).

The fact that recombinant HMG-D increases the nucleosome repeat length (NRL) in a cell-free chromatin assembly system strongly supports this hypothesis. The NRL is strongly dependent on the ionic environment such that polycations are particularly effective in increasing the average separation between adjacent nucleosomes. In accordance with these findings the data implicate the polycationic basic region (residues 85-99; net charge, +10) of HMG-D in this function. However, the HMG-D-dependent increase in NRL is mediated both by the full-length protein and by HMG-D¹⁰⁰. These forms differ substantially in net charge +7 (for HMG-D) and +17 (for HMG-D¹⁰⁰), suggesting that the chromatin DNA can compete effectively with the polyanionic acidic tail of HMG-D. Histone H1 and the HMGN1 and HMGN2 proteins (formerly HMG-14 and HMG-17) are the only other proteins reported to cause such a change, in the case of H1 presumably by binding to the linker DNA. The binding of H1 to the linker sequence appears to differ from that of HMG-D. Increasing concentrations of histone H1 added to the assembly reaction will continue to increase the NRL to well over 220 bp before the regular nucleosomal array is lost. HMG-D, on the other hand, increases the NRL to only ~180 bp. This may reflect the stoichiometry of binding to the linker sequence. Di-nucleosomal DNA reconstituted by dialysis has been shown to be able to bind two molecules of H1 but only a single molecule of HMGB1. Although the exact nature of the binding remains unknown, HMG-D binds ~14 bp of DNA, and consequently 1-2 molecules of HMG-D could potentially occupy the linker space (Ner, 2001).

A tight correlation between nucleosome spacing and the folding of the nucleosomal fiber into a 30-nm fiber has been observed, which led to the suggestion that different NRLs would correspond to particular fiber geometries and, therefore, compaction states. Accordingly, increased nucleosome spacing is indicative of more compacted chromatin. The observation that HMG-D does not increase the NRL beyond 185 bp as H1 may indicate that HMG-D-containing chromatin is folded but is less compacted (Ner, 2001).

Like other HMG domain proteins such as LEF-1 and SRY, HMG-D can introduce sharp bends or kinks into DNA. The current estimates of the magnitude of the DNA kinks induced by HMG-D range from 100-120° for the full-length protein to 60° to >90° for HMG-D¹⁰⁰. These values are substantially greater than the average curvature of DNA wrapped around the histone octamer and indicate that HMG-D bound DNA is not smoothly curved. In the context of linker DNA, such a state would be consistent with both the lack of UV-induced thymine dimer formation in the linker and also, with evidence from electric dichroism studies, that the trajectory of linker DNA differs from that of DNA bound to the core histones. Of particular relevance are the observations that, in the presence of histone H1 derivatives containing a major proportion of the basic C-terminal domain, the linker DNA enters and leaves a single chromatosome as a straight rod approximately perpendicular to the superhelical axis. A similar structure has been observed in chromatin fibers. This organization implies that the DNA must bend sharply as it enters and leaves the chromatosome. A possible role for HMG-D would be to induce such sharp bends by kinking the DNA and thereby promoting a higher level of chromatin folding (Ner, 2001).

Evidence has been provided for an interaction of HMGB1 with the nucleosome and it has been suggested that it might replace histone H1 in the nucleosome. Evidence has been provided for interactions between histone H1 and HMGB1. The results are consistent with these observations. (1) In a Far Western analysis, H1 is the predominant protein identified when labeled HMG-D was used as a probe. (2) Using chromatin assembled on DNA attached to paramagnetic beads and preloaded with HMG-D protein, HMG-D is displaced upon titration of histone H1. It is noted that the full-length HMG-D and HMG-D¹⁰⁰ both interact with H1 in a Far Western analysis. The alanine-lysine-rich region (amino acids 84-100, AKKRAKPAKKVAKKSKK) is very similar to a region found in histone H1. Far Western analysis suggests that this region, or possibly the region immediately preceding glycine-rich linker, is interacting with H1. In HMG-D this sequence contains a serine residue that is phosphorylated by casein kinase II.

Although it is possible to argue for a structural role for HMG-D and HMGB1 in early embryonic chromatin, in vitro observations show that in the absence of H1 HMG-D, although initially present at high levels, is displaced to below 1 molecule/10-20 nucleosomes as the reaction proceeds and the chromatin matures. This would argue against a purely structural role for HMG-D and suggest that the protein may fulfill a different role. One possibility is that HMG-D functions as a chaperone molecule and preconfigures the DNA to facilitate the chromatin assembly process. HMG-D could participate to bend the DNA at the exit and entry points to the nucleosome, and this bend is then stabilized by histone H1. Under such a scenario, as chromatin assembly proceeds and the core histones are recruited, HMG-D molecules are displaced. The linker sequences would be the only locations where the protein would persist for longer duration. However, this too would be displaced on the addition of other chromatin-associated proteins (transcription factors, assembly factors). Such a mechanism would be very similar to that proposed for the recruitment of transcription factors. Similarly the displacement and competition with histone H1 can be envisaged as part of a process in which the DNA is kinked by HMG-D, and then the binding of the linker histone stabilizes this kink (Ner, 2001).

Preblastoderm embryonic chromatin clearly differs profoundly from post-blastoderm chromatin. Early syncytial nuclei are much larger and contain chromatin that is less compacted than later nuclei. In the early embryo HMG-D is highly abundant, although not all molecules are necessarily available for DNA binding. It is deposited in the egg by the mother but thereafter is maintained at an approximately constant level per embryo. Consequently, with each nuclear division the average number of HMG-D molecules per nucleus falls, although during nuclear cycles 7-14 the amount of H1 rapidly increases. Only during cycle 7 does the size of the nuclei begin to decrease. By cycles 10-12 a sufficient amount of histone H1 has accumulated to allow the reorganization of chromatin to a transcriptionally active state. Subsequently, increased zygotic transcription elevates histone H1 levels further. This exponential increase of histone H1 together with the increasing number of nuclei rapidly deplete HMG-D protein to levels that cannot have global effects on chromatin structure. What could be the physiological significance of different linker proteins? HMG-D- or H1-containing chromatin may differ profoundly in the degree or mode of compaction. The looser structure formed in the absence of H1 could facilitate the rapid condensation and decondensation required during the very short early cleavage cycles (Ner, 2001).

The switch from HMG-D- to H1-containing chromatin correlates with the acquisition of global transcriptional competence. Similar observations have been described in the Xenopus system in which B4, an H1 variant, and HMGB1 disappear during mid-blastula transition, again correlating with a change in the accessibility of embryonic chromatin to class III transcriptional machinery. The cell-free system employed in this study may facilitate the detailed analysis of this major switch in genome function during embryonic development (Ner, 2001).

Adult

A genomic fragment was cloned from a DNA library constructed from a Drosophila enhancer trap line in which reporter gene expression was observed at the anterior-most tip of the ovaries and testes. This genomic clone was identified as the L-repeat of the Drosophila melanogaster histone gene cluster. Northern blotting and in situ hybridization to RNA in tissues with individual cDNAs and PCR-generated probes for each histone confirm that gene expression is greatest at the anterior portion of each ovariole, in the germarium, and is also elevated in a few individual nurse cells and somatic follicle cells within the egg chamber during early developmental stages. Histone H1 and each of the core histones have a similar expression pattern that is correlated to cell division. Maternal stores of histone transcripts are also transported to the mature oocyte from the nurse cells at a later stage of oogenesis (stage 10), when virtually all the nurse cells contain high levels of histone transcripts. The results are consistent with expression of the somatic histone gene cluster during oogenesis as a coordinate unit. There does not seem to be a reduced level of somatic type H1 in the germ-line, as is observed in some other species. The relationship between the P[lacZ] expression pattern in the germarium and the overall expression of the histone cluster suggests there are specific regulatory elements for germ-line expression (Walker, 1998).

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date revised: 1 September 2020

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