Faculty Opinions recommendation of Relationship between histone H3 lysine 9 methylation, transcription repression, and heterochromatin protein 1 recruitment.

2005 ◽  
Author(s):  
Fyodor Urnov
Keyword(s):  
Histone H3 ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Transcription Repression

Dynamic variation of histone H3 trimethyl Lys4 (H3K4me3) and heterochromatin protein 1 (HP1) with employment length in nickel smelting workers

Biomarkers ◽  
2016 ◽  
Vol 22 (5) ◽  
pp. 420-428 ◽  
Author(s):  
Yanhong Zhao ◽  
Ning Cheng ◽  
Min Dai ◽  
Hongquan Pu ◽  
Tongzhang Zheng ◽  
...  
Keyword(s):  
Histone H3 ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Dynamic Variation ◽  
Nickel Smelting

scholarly journals Pericentromeric Heterochromatin Domains Are Maintained without Accumulation of HP1

2007 ◽  
Vol 18 (4) ◽  
pp. 1464-1471 ◽  
Author(s):  
Julio Mateos-Langerak ◽  
Maartje C. Brink ◽  
Martijn S. Luijsterburg ◽  
Ineke van der Kraan ◽  
Roel van Driel ◽  
...  
Keyword(s):  
Histone H3 ◽  
Dominant Negative ◽  
Pericentromeric Heterochromatin ◽  
Heterochromatin Protein 1 ◽  
Dapi Staining ◽  
Heterochromatin Protein ◽  
3T3 Fibroblasts ◽  
Heterochromatin Structure ◽  
Hp1 Proteins

The heterochromatin protein 1 (HP1) family is thought to be an important structural component of heterochromatin. HP1 proteins bind via their chromodomain to nucleosomes methylated at lysine 9 of histone H3 (H3K9me). To investigate the role of HP1 in maintaining heterochromatin structure, we used a dominant negative approach by expressing truncated HP1α or HP1β proteins lacking a functional chromodomain. Expression of these truncated HP1 proteins individually or in combination resulted in a strong reduction of the accumulation of HP1α, HP1β, and HP1γ in pericentromeric heterochromatin domains in mouse 3T3 fibroblasts. The expression levels of HP1 did not change. The apparent displacement of HP1α, HP1β, and HP1γ from pericentromeric heterochromatin did not result in visible changes in the structure of pericentromeric heterochromatin domains, as visualized by DAPI staining and immunofluorescent labeling of H3K9me. Our results show that the accumulation of HP1α, HP1β, and HP1γ at pericentromeric heterochromatin domains is not required to maintain DAPI-stained pericentromeric heterochromatin domains and the methylated state of histone H3 at lysine 9 in such heterochromatin domains.

Phosphorylation of histone H3 by Haspin regulates chromosome alignment and segregation during mitosis in maize

2020 ◽  
Author(s):  
Yang Liu ◽  
Chunhui Wang ◽  
Handong Su ◽  
James A Birchler ◽  
Fangpu Han
Keyword(s):  
Chromosome Segregation ◽  
Histone H3 ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Factor B ◽  
Microtubule Attachment ◽  
Chromosome Alignment ◽  
Chromosomal Passenger ◽  
Mitosis And Meiosis

Abstract In human cells, Haspin-mediated histone H3 threonine 3 (H3T3) phosphorylation promotes centromeric localization of the chromosomal passenger complex, thereby ensuring proper kinetochore–microtubule attachment. Haspin also binds to PDS5 cohesin-associated factor B (Pds5B), antagonizing the Wings apart-like protein homolog (Wapl)–Pds5B interaction and thus preventing Wapl from releasing centromeric cohesion during mitosis. However, the role of Haspin in plant chromosome segregation is not well understood. Here, we show that in maize (Zea mays) mitotic cells, ZmHaspin localized to the centromere during metaphase and anaphase, whereas it localized to the telomeres during meiosis. These results suggest that ZmHaspin plays different roles during mitosis and meiosis. Knockout of ZmHaspin led to decreased H3T3 phosphorylation and histone H3 serine 10 phosphorylation, and defects in chromosome alignment and segregation in mitosis. These lines of evidence suggest that Haspin regulates chromosome segregation in plants via the mechanism described for humans, namely, H3T3 phosphorylation. Plant Haspin proteins lack the RTYGA and PxVxL motifs needed to bind Pds5B and heterochromatin protein 1, and no obvious cohesion defects were detected in ZmHaspin knockout plants. Taken together, these results highlight the conserved but slightly different roles of Haspin proteins in cell division in plants and in animals.

scholarly journals HP1 Binding to Chromatin Methylated at H3K9 Is Enhanced by Auxiliary Factors

2006 ◽  
Vol 27 (2) ◽  
pp. 453-465 ◽  
Author(s):  
Ragnhild Eskeland ◽  
Anton Eberharter ◽  
Axel Imhof
Keyword(s):  
Histone H3 ◽  
Chromatin Modifications ◽  
Multiple Target ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Heterochromatin Formation ◽  
Condensed Form ◽  
Target Sites ◽  
Reconstituted System

ABSTRACT A large portion of the eukaryotic genome is packaged into transcriptionally silent heterochromatin. Several factors that play important roles during the establishment and maintenance of this condensed form have been identified. Methylation of lysine 9 within histone H3 and the subsequent binding of the chromodomain protein heterochromatin protein 1 (HP1) are thought to initiate heterochromatin formation in vivo and to propagate a heterochromatic state lasting through several cell divisions. For the present study we analyzed the binding of HP1 to methylated chromatin in a fully reconstituted system. In contrast to its strong binding to methylated peptides, HP1 binds only weakly to methylated chromatin. However, the addition of recombinant SU(VAR) protein, such as ACF1 or SU(VAR)3-9, facilitates HP1 binding to chromatin methylated at lysine 9 within the H3 N terminus (H3K9). We propose that HP1 has multiple target sites that contribute to its recognition of chromatin, only one of them being methylated at H3K9. These findings have implications for the mechanisms of recognition of specific chromatin modifications in vivo.

scholarly journals How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1460
Author(s):  
Raquel Sales-Gil ◽  
Paola Vagnarelli
Keyword(s):  
Recent Literature ◽  
Histone H3 ◽  
Chromatin Binding ◽  
Heterochromatin Protein 1 ◽  
Binding Ability ◽  
Heterochromatin Protein ◽  
Post Translational Modifications ◽  
Heterochromatin Formation

Heterochromatin Protein 1 (HP1) is a highly conserved protein that has been used as a classic marker for heterochromatin. HP1 binds to di- and tri-methylated histone H3K9 and regulates heterochromatin formation, functions and structure. Besides the well-established phosphorylation of histone H3 Ser10 that has been shown to modulate HP1 binding to chromatin, several studies have recently highlighted the importance of HP1 post-translational modifications and additional epigenetic features for the modulation of HP1-chromatin binding ability and heterochromatin formation. In this review, we summarize the recent literature of HP1 post-translational modifications that have contributed to understand how heterochromatin is formed, regulated and maintained.

scholarly journals The role of heterochromatin in centromere function

2005 ◽  
Vol 360 (1455) ◽  
pp. 569-579 ◽  
Author(s):  
Alison L Pidoux ◽  
Robin C Allshire
Keyword(s):  
Fission Yeast ◽  
Histone H3 ◽  
Centromeric Heterochromatin ◽  
Chromatin Domain ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Centromere Function ◽  
Kinetochore Assembly ◽  
Histone H3 Variant

Chromatin at centromeres is distinct from the chromatin in which the remainder of the genome is assembled. Two features consistently distinguish centromeres: the presence of the histone H3 variant CENP-A and, in most organisms, the presence of heterochromatin. In fission yeast, domains of silent ‘heterochromatin’ flank the CENP-A chromatin domain that forms a platform upon which the kinetochore is assembled. Thus, fission yeast centromeres resemble their metazoan counterparts where the kinetochore is embedded in centromeric heterochromatin. The centromeric outer repeat chromatin is underacetylated on histones H3 and H4, and methylated on lysine 9 of histone H3, which provides a binding site for the chromodomain protein Swi6 (orthologue of Heterochromatin Protein 1, HP1). The remarkable demonstration that the assembly of repressive heterochromatin is dependent on the RNA interference machinery provokes many questions about the mechanisms of this process that may be tractable in fission yeast. Heterochromatin ensures that a high density of cohesin is recruited to centromeric regions, but it could have additional roles in centromere architecture and the prevention of merotely, and it might also act as a trigger for kinetochore assembly. In addition, we discuss an epigenetic model for ensuring that CENP-A is targeted and replenished at the kinetochore domain.

scholarly journals Revisiting the role of heterochromatin protein 1 in DNA repair

2009 ◽  
Vol 185 (4) ◽  
pp. 573-575 ◽  
Author(s):  
Alexander R. Ball ◽  
Kyoko Yokomori
Keyword(s):  
Dna Damage Response ◽  
Histone H3 ◽  
Direct Interaction ◽  
Epigenetic Mark ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Damage Response ◽  
The One ◽  
Methylated Lysine

Heterochromatin protein 1 (HP1) is a conserved factor critical for heterochromatin organization and gene silencing. It is recruited to chromatin by its direct interaction with H3K9me (methylated lysine 9 residue of histone H3), an epigenetic mark for silenced chromatin. Now, Luijsterburg et al. (Luijsterburg, M.S., C. Dinant, H. Lans, J. Stap, E. Wiernasz, S. Lagerwerf, D.O. Warmerdam, M. Lindh, M.C. Brink, J.W. Dobrucki, et al. 2009. J. Cell Biol. 185:577–586) reveal a new H3K9me-independent role for HP1 in the DNA damage response, which is distinct from the one recently reported by Ayoub et al. (Ayoub, N., A.D. Jeyasekharan, J.A. Bernal, and A.R. Venkitaraman. 2008. Nature. 453:682–686).

scholarly journals Physical modeling of the heritability and maintenance of epigenetic modifications

2020 ◽  
Vol 117 (34) ◽  
pp. 20423-20429 ◽  
Author(s):  
Sarah H. Sandholtz ◽  
Quinn MacPherson ◽  
Andrew J. Spakowitz
Keyword(s):  
Gene Expression ◽  
Physical Modeling ◽  
Histone H3 ◽  
Epigenetic Modifications ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Chromosomal Organization ◽  
Chromatin Compaction ◽  
Physical Mechanisms ◽  
Epigenetic Code

We develop a predictive theoretical model of the physical mechanisms that govern the heritability and maintenance of epigenetic modifications. This model focuses on a particular modification, methylation of lysine-9 of histone H3 (H3K9), which is one of the most representative and critical epigenetic marks that affects chromatin organization and gene expression. Our model combines the effect of segregation and compaction on chromosomal organization with the effect of the interaction between proteins that compact the chromatin (heterochromatin protein 1) and the methyltransferases that affect methyl spreading. Our chromatin model demonstrates that a block of H3K9 methylations in the epigenetic sequence determines the compaction state at any particular location in the chromatin. Using our predictive model for chromatin compaction, we develop a methylation model to address the reestablishment of the methylation sequence following DNA replication. Our model reliably maintains methylation over generations, thereby establishing the robustness of the epigenetic code.

scholarly journals Identification of Genes Encoding CENP-A and Heterochromatin Protein 1 of Lipomyces starkeyi and Functional Analysis Using Schizosaccharomyces pombe

Genes ◽  
2020 ◽  
Vol 11 (7) ◽  
pp. 769
Author(s):  
Yuko Takayama
Keyword(s):  
Histone H3 ◽  
Specific Protein ◽  
Lipomyces Starkeyi ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Heterochromatin Formation ◽  
Histone H3 Variant ◽  
Genes Encoding ◽  
Almost All ◽  
Heterochromatin Structure

Centromeres function as a platform for the assembly of multiple kinetochore proteins and are essential for chromosome segregation. An active centromere is characterized by the presence of a centromere-specific histone H3 variant, CENP-A. Faithful centromeric localization of CENP-A is supported by heterochromatin in almost all eukaryotes; however, heterochromatin proteins have been lost in most Saccharomycotina. Here, identification of CENP-A (CENP-AL.s.) and heterochromatin protein 1 (Lsw1) in a Saccharomycotina species, the oleaginous yeast Lipomyces starkeyi, is reported. To determine if these proteins are functional, the proteins in S. pombe, a species widely used to study centromeres, were ectopically expressed. CENP-AL.s. localizes to centromeres and can be replaced with S. pombe CENP-A, indicating that CENP-AL.s. is a functional centromere-specific protein. Lsw1 binds at heterochromatin regions, and chromatin binding is dependent on methylation of histone H3 at lysine 9. In other species, self-interaction of heterochromatin protein 1 is thought to cause folding of chromatin, triggering transcription repression and heterochromatin formation. Consistent with this, it was found that Lsw1 can self-interact. L. starkeyi chromatin contains the methylation of histone H3 at lysine 9. These results indicated that L. starkeyi has a primitive heterochromatin structure and is an attractive model for analysis of centromere heterochromatin evolution.

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