Heterochromatin protein 1: a pervasive controlling influence

Hiragami, K.; Festenstein, Richard

doi:10.1007/s00018-005-5287-9

Cited by 120 publications

(126 citation statements)

References 154 publications

(226 reference statements)

Supporting

Mentioning

121

Contrasting

Order By: Relevance

“…These results indicate that chromosomal association of HP1c is largely determined by the recognition of specific DNA sequences, which is in contrast to the situation observed in the case of Drosophila HP1a, or mammalian HP1␣, where chromosomal association was found to depend on The observed correlations are compared with the range expected if no genes were coregulated and if all were coregulated. the recognition of a specific pattern of histone modifications; namely, H3K9 methylation (Hiragami and Festenstein 2005;Hediger and Gasser 2006). Several HP1 proteins, including HP1a and HP1␣, were reported to interact with a number of transcription factors, replication proteins, and chromatin assembly complexes (Hiragami and Festenstein 2005;Hediger and Gasser 2006;Lomberk et al 2006).…”

Section: Binding Of Hp1c To Chromatin Relies On the Zinc-finger Protementioning

confidence: 99%

“…the recognition of a specific pattern of histone modifications; namely, H3K9 methylation (Hiragami and Festenstein 2005;Hediger and Gasser 2006). Several HP1 proteins, including HP1a and HP1␣, were reported to interact with a number of transcription factors, replication proteins, and chromatin assembly complexes (Hiragami and Festenstein 2005;Hediger and Gasser 2006;Lomberk et al 2006). Yet, it is unclear whether these interactions mediate recruitment of HP1 to specific sites, and/or in response to particular processes, or they actually take place after recruitment to regulate their functions.…”

Section: Binding Of Hp1c To Chromatin Relies On the Zinc-finger Protementioning

confidence: 99%

“…Most frequently, regulation by chromatin involves the establishment of specific patterns of post-translational histone modifications, which result in recruitment of regulatory nonhistone proteins (Ruthenburg et al 2007). Heterochromatin protein 1 (HP1) constitutes one of the best-studied examples (Hiragami and Festenstein 2005;Hediger and Gasser 2006;Lomberk et al 2006), where a regulatory nonhistone protein is recruited to chromatin through the recognition of a specific histone modification, dior trimethylation of Lys 9 on the histone H3 tail (H3K9me2,3). This interaction, which involves the Nterminal chromodomain of HP1, is known to play a fundamental role in the formation and maintenance of heterochromatic domains.…”

mentioning

confidence: 99%

“…Except in budding yeast, HP1 is widely conserved in eukaryotes, with most species containing several isoforms (Hiragami and Festenstein 2005;Lomberk et al 2006). HP1 proteins are characterized by a common structural organization consisting of two conserved domains, the N-terminal chromodomain and the C-terminal chromo-shadow domain, which are spaced by a variable nonconserved hinge domain.…”

mentioning

confidence: 99%

“…Most of our knowledge about the mechanisms of action of HP1 proteins derives from studies addressing the functional properties of Drosophila HP1a or mammalian HP1␣. From these studies, a general picture emerges by which, through the chromodomain, HP1 proteins bind chromatin regions enriched in H3K9me2,3 while, through the chromo-shadow domain, recruiting different factors resulting in various functional outcomes; namely, heterochromatin assembly and gene silencing (Hiragami and Festenstein 2005;Hediger and Gasser 2006;Lomberk et al 2006). It is uncertain whether this general picture applies to all HP1 proteins and possible scenarios.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Drosophila HP1c isoform interacts with the zinc-finger proteins WOC and Relative-of-WOC to regulate gene expression

Font-Burgada¹,

Rossell²,

Auer³

et al. 2008

Genes Dev.

129

View full text Add to dashboard Cite

Heterochromatin protein 1 (HP1) proteins are conserved in eukaryotes, with most species containing several isoforms. Based on the properties of Drosophila HP1a, it was proposed that HP1s bind H3K9me2,3 and recruit factors involved in heterochromatin assembly and silencing. Yet, it is unclear whether this general picture applies to all HP1 isoforms and functional contexts. Here, we report that Drosophila HP1c regulates gene expression, as (1) it localizes to active chromatin domains, where it extensively colocalizes with the poised form of RNApolymerase II (RNApol II), Pol IIo ser5 , and H3K4me3, suggesting a contribution to transcriptional regulation; (2) its targeting to a reporter gene does not induce silencing but, on the contrary, increases its expression, and (3) it interacts with the zinc-finger proteins WOC (without children) and Relative-of-WOC (ROW), which are putative transcription factors. Here, we also show that, although HP1c efficiently binds H3K9me2,3 in vitro, its binding to chromatin strictly depends on both WOC and ROW. Moreover, expression profiling indicates that HP1c, WOC, and ROW regulate a common gene expression program that, in part, is executed in the context of the nervous system. From this study, which unveils the essential contribution of DNA-binding proteins to HP1c functionality and recruitment, HP1 proteins emerge as an increasingly diverse family of chromatin regulators.[Keywords: HP1; WOC; ROW/CG8092; chromatin; Drosophila] Supplemental material is available at http://www.genesdev.org.

show abstract

Section: Binding Of Hp1c To Chromatin Relies On the Zinc-finger Protementioning

confidence: 99%

Section: Binding Of Hp1c To Chromatin Relies On the Zinc-finger Protementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Drosophila HP1c isoform interacts with the zinc-finger proteins WOC and Relative-of-WOC to regulate gene expression

Font-Burgada¹,

Rossell²,

Auer³

et al. 2008

Genes Dev.

129

View full text Add to dashboard Cite

show abstract

The HP1a Disordered C Terminus and Chromo Shadow Domain Cooperate to Select Target Peptide Partners

et al. 2011

View full text Add to dashboard Cite

Drosophila melanogaster Heterochromatin Protein 1a (HP1a) is essential for compacted heterochromatin structure and associated gene silencing. Its chromo shadow domain (CSD) is well-known for binding to peptides that contain a PXVXL motif. Heterochromatin protein 2 (HP2) is a nonhistone chromosomal protein that associates with HP1a in the pericentric heterochromatin, telomeres and the fourth chromosome. Using NMR spectroscopy, fluorescence polarization and site-directed mutagenesis, we identified an LCVKI motif in HP2 that binds to the HP1a CSD. The binding affinity of the HP2 fragment is approximately two orders of magnitude higher than that of peptides from PIWI (with a PRVKV motif), AF10 (with a PLVVL motif), or CG15356 (with LYPLL and LSIVA motifs). To delineate differential interactions of the HP1a CSD, we characterized its structure, backbone dynamics and dimerization constant. We find that the dimerization constant is bracketed by the affinities of HP2 and PIWI, which dock to the same HP1a homodimer surface. This suggests that HP2, but not PIWI, interaction can drive homodimerization of HP1a. Interestingly, the integrity of the disordered C-terminal extension (CTE) of HP1a is essential for discriminatory binding, whereas swapping the PXVXL motifs does not confer specificity. Serine phosphorylation at the peptide binding surface of the CSD is thought to regulate heterochromatin assembly. Glutamic acid substitution at these sites destabilizes HP1a dimers, but improves the interaction with both binding partners. Our studies underscore the importance of CSD dimerization and cooperation with the CTE in forming distinct complexes of HP1a.

show abstract

Interaction of PGC7 and HP1BP3 Maintains Meg3‐DMR Methylation by Regulating Chromatin Configuration

Liu,

Hao,

Huang

et al. 2024

J of Cellular Biochemistry

View full text Add to dashboard Cite

Genomic imprinting is essential for mammalian development. PGC7, an important maternal factor, binds to dimethylated histone H3K9 (H3K9me2), maintaining DNA methylation in zygotes and stem cells. However, the underlying molecular mechanisms of PGC7‐maintained genomic imprinting in stem cells are not clear. Our previous study has identified that PGC7 interacts with HP1BP3, a novel member of the histone H1 family. In this study, we found that PGC7 interacts with the central globular domain of HP1BP3 through its C‐terminal tail and that HP1BP3 is responsible for the recruitment of PGC7 at the Meg3 differentially methylated region (DMR) in the Dlk1–Dio3 imprinted domain. HP1BP3 or PGC7 depletion decreases enrichment in the Meg3‐DMR, leading to DNA hypermethylation in this region. Moreover, the cooperative binding of PGC7 and HP1BP3 can antagonize the enrichment of DNMT3A in the Meg3‐DMR, and the depletion of HP1BP3 or PGC7 separately induces chromosome decondensation in this region. In summary, this is the first study demonstrating that PGC7 and HP1BP3 synergistically maintain the methylation status of the Meg3‐DMR by enabling a chromatin configuration that interferes with the binding of the de novo DNA methyltransferase DNMT3A.

show abstract

Heterochromatin protein 1: a pervasive controlling influence

Cited by 120 publications

References 154 publications

Drosophila HP1c isoform interacts with the zinc-finger proteins WOC and Relative-of-WOC to regulate gene expression

Drosophila HP1c isoform interacts with the zinc-finger proteins WOC and Relative-of-WOC to regulate gene expression

The HP1a Disordered C Terminus and Chromo Shadow Domain Cooperate to Select Target Peptide Partners

Interaction of PGC7 and HP1BP3 Maintains Meg3‐DMR Methylation by Regulating Chromatin Configuration

Contact Info

Product

Resources

About