The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
HP1 Binds Specifically to Lys26-methylated Histone H1.4, whereas Simultaneous Ser27 Phosphorylation Blocks HP1 Binding
Open accessAbstract
Histone lysine methylation can have positive or negative effects on transcription, depending on the precise methylation site. According to the "histone code" hypothesis these methylation marks can be read by proteins that bind them specifically and then regulate downstream events. Hetero-chromatin protein 1 (HP1), an essential component of heterochromatin, binds specifically to methylated Lys(9) of histone H3 (K9/H3). The linker histone H1.4 is methylated on Lys(26) (K26/H1.4), but the role of this methylation in downstream events remains unknown. Here we identify HP1 as a protein specifically recognizing and binding to methylated K26/H1.4. We demonstrate that the Chromo domain of HP1 is mediating this binding and that phosphorylation of Ser(27) on H1.4 (S27/H1.4) prevents HP1 from binding. We suggest that methylation of K26/H1.4 could have a role in tethering HP1 to chromatin and that this could also explain how HP1 is targeted to those regions of chromatin where it does not colocalize with methylated K9/H3. Our results provide the first experimental evidence for a "phospho switch" model in which neighboring phosphorylation reverts the effect of histone lysine methylation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
Cited by
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Polycomb silencers control cell fate, development and cancer
Sparmann, A., & van Lohuizen, M. (2006) · Nature Reviews Cancer · doi:10.1038/nrc1991 · Cited by 1,303
Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions
Bracken, A. P., Dietrich, N., Pasini, D., Hansen, K. H., & Helin, K. (2006) · Genes & Development · doi:10.1101/gad.381706 · Cited by 1,257
Emerging roles of linker histones in regulating chromatin structure and function
Fyodorov, D. V., Zhou, B.-R., Skoultchi, A. I., & Bai, Y. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.94 · Cited by 485
Chromatin higher-order structures and gene regulation
Li, G., & Reinberg, D. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.01.022 · Cited by 454
Metadata
- Authors
- Daujat, S., Zeissler, U., Waldmann, T., Happel, N., & Schneider, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-11
- Volume
- 280
- Issue
- 45
- Pages
- 38090-38095
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2041787701
- Cited by
- 230
- References
- 1
- FWCI
- 3.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: HP1 Binds Specifically to Lys26-methylated Histone H1.4, whereas Simultaneous Ser27 Phosphorylation Blocks HP1 Binding. https://app.cochat.ai/papers/10.1074/jbc.c500229200
- The paper
- Daujat, S., Zeissler, U., Waldmann, T., Happel, N., & Schneider, R. (2005). HP1 Binds Specifically to Lys26-methylated Histone H1.4, whereas Simultaneous Ser27 Phosphorylation Blocks HP1 Binding. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.c500229200
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
