Chromatin replication

Gruss, Claudia; Sogo, José M.

doi:10.1002/bies.950140102

Cited by 54 publications

(36 citation statements)

References 57 publications

(12 reference statements)

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“…Our current view of chromatin organization in general attributes an inhibitory function to nucleosomes for processes like DNA replication [62] and transcription [51,63,64]. For this reason one favours mechanistic ideas to explain the disintegration or transient removal of nucleosomes which results in the most accessible form of genetic information-free DNA.…”

Section: Evidences Perspectivesmentioning

confidence: 99%

Histone deacetylase

et al. 1993

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Core histones can be modified by reversible, posttranslational acetylation of specific lysine residues within the N-terminal protein domains. The dynamic equilibrium of acetylation is maintained by two enzyme activities, histone acetyltransferase and histone deacetylase. Recent data on histone deacetylases and on anionic motifs in chromatin-or DNA-binding regulatory proteins (e.g. transcription factors, nuclear proto-oncogenes) are summarized and united into a hypothesis which attributes a key function to histone deacetylation for the binding of regulatory proteins to chromatin by a transient, specific local increase of the positive charge in the N-terminal domains of nucleosomal core histones. According to our model, the rapid deacetylation of distinct lysines in especially H2A and H2B would facilitate the association of anionic protein domains of regulatory proteins to specific nucleosomes. Therefore histone deacetylation (histone deacetylases) may represent a unique regulatory mechanism in the early steps of gene activation, in contrast to the more structural role of histone acetylation (histone acetyltransferases) for nucleosomal transitions during the actual transcription process.

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Section: Evidences Perspectivesmentioning

confidence: 99%

Histone deacetylase

et al. 1993

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“…In the G1 and G2 phases of the cell cycle, DNMT1 remains diffused throughout the nucleoplasm, but associates with replication foci during S phase (Leonhardt et al 1992;Liu et al 1998). Movement of the replication machinery transiently disrupts the chromatin fiber and leads to the random segregation of the parental nucleosomes among the two daughter strands (Gruss and Sogo 1992). Additional nucleosomes are added onto the newly synthesized DNA via deposition of newly synthesized histone (H3/H4) 2 tetramers followed by H2A/H2B dimers (Jackson 1990;Gruss et al 1993).…”

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confidence: 99%

Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication

Estève¹,

Chin²,

Smallwood³

et al. 2006

Genes Dev.

481

408

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Chromatin methylation is necessary for stable repression of gene expression during mammalian development. During cell division, DNMT1 maintains the DNA methylation pattern of the newly synthesized daughter strand, while G9a methylates H3K9. Here, DNMT1 is shown to directly bind G9a both in vivo and in vitro and to colocalize in the nucleus during DNA replication. The complex of DNMT1 and G9a colocalizes with dimethylated H3K9 (H3K9me2) at replication foci. Similarly, another H3K9 histone methyltransferase, SUV39H1, colocalizes with DNMT1 on heterochromatic regions of the nucleoli exclusively before cell division. Both DNMT1 and G9a are loaded onto the chromatin simultaneously in a ternary complex with loading factor PCNA during chromatin replication. Small interfering RNA (siRNA) knockdown of DNMT1 impairs DNA methylation, G9a loading, and H3K9 methylation on chromatin and rDNA repeats, confirming DNMT1 as the primary loading factor. Additionally, the complex of DNMT1 and G9a led to enhanced DNA and histone methylation of in vitro assembled chromatin substrates. Thus, direct cooperation between DNMT1 and G9a provides a mechanism of coordinated DNA and H3K9 methylation during cell division.[Keywords: DNMT1; G9a; SUV39H1; methylation; chromatin; replication] Supplemental material is available at http://www.genesdev.org.

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“…Hence, in the analysis of the vast array of nuclear processes that involve DNA, it is essential to consider the role of chromatin structure and assembly (for reviews, see: Dilworth & Dingwall 1988;van Holde 1989;Svaren & Chalkley 1990;Gruss & Sogo 1992;Krude 1995;Sogo & Laskey 1995;Wolffe 1995;Annunziato 1995;Roth & Allis 1996;Kaufman 1996;Grunstein 1997).…”

Section: Introductionmentioning

confidence: 99%

Chromatin assembly factors: a dual function in nucleosome formation and mobilization?

1997

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Chromatin assembly is a process that interfaces DNA replication, gene expression and progression through the cell cycle, and it is therefore critically involved in many important biological phenomena. This brief review provides a general background to the study of chromatin assembly, as well as an overview of putative chromatin assembly factors. Interestingly, recent data suggest that the ATP-utilizing chromatin assembly factor, ACF, functions not only in nucleosome formation, but also in the ATP-dependent remodelling of chromatin that facilitates DNAutilizing processes, such as transcription, replication, recombination, and repair.

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Chromatin replication

Cited by 54 publications

References 57 publications

Histone deacetylase

Histone deacetylase

Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication

Chromatin assembly factors: a dual function in nucleosome formation and mobilization?

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