ArticleProceedings of the National Academy of Sciences of the United States of America2013
Posttranslational modification of CENP-A influences the conformation of centromeric chromatin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed, 129 citations in OpenAlex.
- Modulating Nucleosomal H3 Tail Dynamics with Lysine and Serine Modifications.bioRxiv : the preprint server for biology · 2026Article
- Determinants of centromeric nucleosome conformation.bioRxiv : the preprint server for biology · 2026Article
- Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Review
- Native and tagged CENP-A histones are functionally inequivalent.Epigenetics & chromatin · 2024Article
- Distinct mononuclear diploid cardiac subpopulation with minimal cell-cell communications persists in embryonic and adult mammalian heart.Frontiers of medicine · 2023Article
- Multicomponent Oxidative Nitrile Thiazolidination Reaction for Selective Modification of N-terminal Dimethylation Posttranslational Modification.Journal of the American Chemical Society · 2023Article
- Impact of Protein NLife (Basel, Switzerland) · 2023Review
- EWSR1 maintains centromere identity.Cell reports · 2023Article
- Design and characterization of PROTAC degraders specific to protein N-terminal methyltransferase 1.European journal of medicinal chemistry · 2022Article
- Article
- Centromere Chromatin Dynamics at a Glance.Epigenomes · 2022Review
- Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022Review
- The Roles of Histone Post-Translational Modifications in the Formation and Function of a Mitotic Chromosome.International journal of molecular sciences · 2022Review
- Gene replacement strategies validate the use of functional tags on centromeric chromatin and invalidate an essential role for CENP-ACell reports · 2021Article
- Age-related neurodegeneration and cognitive impairments of NRMT1 knockout mice are preceded by misregulation of RB and abnormal neural stem cell development.Cell death & disease · 2021Article
- Discovering the N-Terminal Methylome by Repurposing of Proteomic Datasets.Journal of proteome research · 2021Article
- Past, present, and perspectives of protein N-terminal methylation.Current opinion in chemical biology · 2021Review
- Chemoproteomic Study Uncovers HemK2/KMT9 As a New Target for NTMT1 Bisubstrate Inhibitors.ACS chemical biology · 2021Article
- Transgenerational inheritance of centromere identity requires the CENP-A N-terminal tail in the C. elegans maternal germ line.PLoS biology · 2021Article
- Modulation of N-terminal methyltransferase 1 by an NBiochemical and biophysical research communications · 2021Article
25 more citing papers are in PubMed but not listed here.
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12 authors at 5 institutions in 3 countries.
Funding
Abstract
Centromeres are chromosomal loci required for accurate segregation of sister chromatids during mitosis. The location of the centromere on the chromosome is not dependent on DNA sequence, but rather it is epigenetically specified by the histone H3 variant centromere protein A (CENP-A). The N-terminal tail of CENP-A is highly divergent from other H3 variants. Canonical histone N termini are hotspots of conserved posttranslational modification; however, no broadly conserved modifications of the vertebrate CENP-A tail have been previously observed. Here, we report three posttranslational modifications on human CENP-A N termini using high-resolution MS: trimethylation of Gly1 and phosphorylation of Ser16 and Ser18. Our results demonstrate that CENP-A is subjected to constitutive initiating methionine removal, similar to other H3 variants. The nascent N-terminal residue Gly1 becomes trimethylated on the α-amino group. We demonstrate that the N-terminal RCC1 methyltransferase is capable of modifying the CENP-A N terminus. Methylation occurs in the prenucleosomal form and marks the majority of CENP-A nucleosomes. Serine 16 and 18 become phosphorylated in prenucleosomal CENP-A and are phosphorylated on asynchronous and mitotic nucleosomal CENP-A and are important for chromosome segregation during mitosis. The double phosphorylation motif forms a salt-bridged secondary structure and causes CENP-A N-terminal tails to form intramolecular associations. Analytical ultracentrifugation of phospho-mimetic CENP-A nucleosome arrays demonstrates that phosphorylation results in greater intranucleosome associations and counteracts the hyperoligomerized state exhibited by unmodified CENP-A nucleosome arrays. Our studies have revealed that the major modifications on the N-terminal tail of CENP-A alter the physical properties of the chromatin fiber at the centromere.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.