Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells

Jackson, Vaughn; Chalkley, Roger

doi:10.1021/bi00345a026

Cited by 69 publications

(43 citation statements)

References 40 publications

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“…In agreement with our global analysis (supplementary material Fig. S1C), and consistent with previous biochemical and FRAP (fluorescence recovery after photobleaching) analyses in human cells (Bönisch et al, 2012;Higashi et al, 2007;Jackson and Chalkley, 1985;Kimura et al, 2006), within the detection range of our method both variants showed a comparable extensive deposition of newly synthesized histones in euchromatin. However, the situation proved to be different at the PHC domains, where the distribution of newly synthesized histones relative to euchromatin could be categorized into one of three distinct patterns -exclusion, even distribution or enrichment (Fig.…”

Section: Different Dynamics Of H2a and H2az Deposition At Phcsupporting

confidence: 93%

“…In contrast to CENP-A, the deposition dynamics of H2A variants at centromeres remain unknown. Notably, H2A variants constantly exchange at a rapid rate throughout the nucleus (Bönisch et al, 2012;Higashi et al, 2007;Jackson and Chalkley, 1985;Kimura et al, 2006), raising an important question regarding their stable maintenance at a given locus. Furthermore, given that H2A.Z displays a broader localization across the genome than CENP-A, its dynamics might be distinct in different genomic compartments.…”

Section: Introductionmentioning

confidence: 99%

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Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Boyarchuk¹,

Filipescu²,

Vassias³

et al. 2014

Journal of Cell Science

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BSTRACTCorrect chromosome segregation requires a unique chromatin environment at centromeres and in their vicinity. Here, we address how the deposition of canonical H2A and H2A.Z histone variants is controlled at pericentric heterochromatin (PHC). Whereas in euchromatin newly synthesized H2A and H2A.Z are deposited throughout the cell cycle, we reveal two discrete waves of deposition at PHC -during mid to late S phase in a replicationdependent manner for H2A and during G1 phase for H2A.Z. This G1 cell cycle restriction is lost when heterochromatin features are altered, leading to the accumulation of H2A.Z at the domain. Interestingly, compromising PHC integrity also impacts upon neighboring centric chromatin, increasing the amount of centromeric CENP-A without changing the timing of its deposition. We conclude that the higher-order chromatin structure at the pericentric domain influences dynamics at the nucleosomal level within centromeric chromatin. The two different modes of rearrangement of the PHC during the cell cycle provide distinct opportunities to replenish one or the other H2A variant, highlighting PHC integrity as a potential signal to regulate the deposition timing and stoichiometry of histone variants at the centromere.

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Section: Different Dynamics Of H2a and H2az Deposition At Phcsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Boyarchuk¹,

Filipescu²,

Vassias³

et al. 2014

Journal of Cell Science

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“…Thus, H2A/H2B may displace more often than H3/H4. This is consistent with the pioneering studies of Jackson and Chalkley (1985) that illustrated that the timing and location of H2A/H2B deposition into chromatin is somewhat different than H3/H4 deposition and was more evident outside of S phase. These early studies may have reflected a more frequent replacement of H2A/H2B than H3/H4 in transcribed chromatin.…”

Section: Nucleosome Displacement During Transcription Elongationsupporting

confidence: 91%

Nucleosome displacement in transcription: Figure 1.

Workman¹

2006

Genes Dev.

277

221

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Recent reports reinforce the notion that nucleosomes are highly dynamic in response to the process of transcription. Nucleosomes are displaced at promoters during gene activation in a process that involves histone modification, ATP-dependent nucleosome remodeling complexes, histone chaperones and perhaps histone variants. During transcription elongation nucleosomes are acetylated and transferred behind RNA polymerase II where they are required to suppress spurious transcription initiation within the body of the gene. It is becoming increasingly clear that the eukaryotic transcriptional machinery is adapted to exploit the presence of nucleosomes in very sophisticated ways. Nucleosome-free regions at gene promotersRemoval of nucleosomes has been a long-standing hypothesis for how genes might become activated, but only recently have experiments begun to rigorously address this topic. For some time after the discovery of DNasehypersensitive sites (DHSs) in chromatin (for review, see Elgin 1981), it was anticipated that these nuclease sensitive regions would correspond to segments along the chromosome that are free of nucleosomes. With the common occurrence of DHSs at known transcriptional regulatory regions such as enhancers and promoters, mapping these exposed sites in genomic DNA became a powerful tool for identifying novel regulatory sites such as locus control regions (LCRs) and other functional genomic sequences (for review see, Gross and Garrard 1988). However, the question of whether these sites were actually histone free or simply did not look like nucleosomes to nucleases remained unresolved. The initial idea that DHSs must be nucleosome-free was attractive since the structure and stability of nucleosomes did not seem likely to accommodate the cobinding of transcription factors (Brown 1984;Kornberg and Lorch 1991). Early support for the notion that at least some of these regions are free of histones came from McGhee and Felsenfeld (McGhee et al. 1981), who examined the chicken adult ␤-globin DHS by restriction endonuclease digestion. They showed the release of a 115-base-pair (bp) fragment from the DHS, of which one-third migrated on gels like naked DNA. In contrast, studies of an inducible DHS at the MMTV promoter suggested that it was still occupied by core histones following induction (Bresnick et al. 1992;Truss et al. 1995), thereby demonstrating the co-occupancy of histones and transcription factors. Moreover, a DHS could be reconstituted by the binding of transcription factors to the HIV-1 enhancer within a nucleosome array without the loss of histones (Steger and Workman 1997;Angelov et al. 2000). Thus, while DHSs do not appear to contain canonical nucleosomes as defined by nuclease digestion, an altered nucleosome or alternative histone DNA complex may still exist at these sites in some instances. Nevertheless, remembering the caveat that DHSs might still be bound by histones, we will refer to these sites as nucleosome-free for the purposes of this review. Nucleosome distribution in Saccharomyces ce...

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“…but not the histones H3 and H4, were actually incorporated into bulk chromatin that was separated from replicating chromatin by various fractionation means [22 -271. The incorporation occurred similarly even at the G1 stage of the cell cycle [32] or even when DNA replication was inhibited by hydroxyurea [33], though the rate of histone synthesis was also lowered under these conditions. Likewise, all five types of histone were synthesized and incorporated into chromatin in lymphocytes at the GO stage in the peripheral circulation [34].…”

Section: Resultsmentioning

confidence: 93%

Heterogeneous assembly of nascent core histones to form nucleosomal histone octamers in mouse FM3A cells

Sugasawa

Ishimi

Yamada

et al. 1989

European Journal of Biochemistry

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We investigated the assembly of newly synthesized histones into nucleosomal histone octamers using an isopycnic centrifugation analysis of these proteins of mouse FM3A cells that had been labeled by culture with heavy amino acids. Cross-linked histone octamers or non-cross-linked core histones were separated electrophoretically from other proteins on sodium dodecyl sulfate/polydcrylamide gels before being banded to equilibrium in cesium formate/guanidinium chloride density gradients. The density of core histones rapidly came to equilibrium after culture of cells in the medium containing heavy amino acids for a time as short as 30 min, indicating that the density of histone octamers in the density-labeled cells reflects the content of these new (dense) core histones relative to old (light) ones in the octamer assembly. Cross-linked histone octamers from these cells were of heterogeneous densities as judged from a broad band in a density gradient. l h e position and width of the band was essentially unaffected, though the peak position of the density distribution within the band moved progressively from a less to a more dense area, when the time of culture was prolonged from 2 h to 16 h. It is concluded, therefore, that new and old histones are assembled into histone octamers in heterogeneous ratios in contradiction to a conservative or semi-conservative assembly model and it is also suggested that incorporation into chromatin of new histones is not necessarily restricted to newly replicated chromatin regions.Eukaryotic nuclear DNA is associated with five types of histones and a number of non-histone proteins to form a basic structural unit, a nucleosome. A nucleosome contains a histone octamer consisting of two sets of four core histones, HZA, H2B, H3 and H4, approximately 200 base pairs of DNA winding around the octamer, a molecule of histone HI and, additionally, a variety of non-histone proteins [ I , 21. Nucleosomes are duplicated as DNA is synthesized in the S phase of the cell division cycle. Certain structural features of nucleosomes have to be reproduced precisely in this course, since activitics of spccific genes, which are inherited from parent to daughter cells, are often dependent on the chromatin structure [3 -81. Moreover, the dynamic structure of nucleosomes in the vicinity of replication forks might be involved in the mcchanism of DNA replication.Several models have been so far proposed for the assembly of newly synthesizcd core histones to form a chromatin structure (Fig. 1). According to the first model, new core histones are not mixed with old ones to form completely new octamers on the replicated DNA [9-141. As for the segregation of preexisting histone octamers at DNA replication forks, however, both conservative [ l l , 12, 151 and dispersive [16-191 segregations have been reported (Fig. 1A). The second model is such that a pre-existing histone octamer is divided into two tetramers, H2A-H2B-H3-H4, each of which is assembled with a set of new core histones to form hybrid octamers on both rep...

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Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells

Cited by 69 publications

References 40 publications

Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Nucleosome displacement in transcription: Figure 1.

Heterogeneous assembly of nascent core histones to form nucleosomal histone octamers in mouse FM3A cells

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