The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
PARP1 ADP-ribosylates lysine residues of the core histone tails
Open accessAbstract
The chromatin-associated enzyme PARP1 has previously been suggested to ADP-ribosylate histones, but the specific ADP-ribose acceptor sites have remained enigmatic. Here, we show that PARP1 covalently ADP-ribosylates the amino-terminal histone tails of all core histones. Using biochemical tools and novel electron transfer dissociation mass spectrometric protocols, we identify for the first time K13 of H2A, K30 of H2B, K27 and K37 of H3, as well as K16 of H4 as ADP-ribose acceptor sites. Multiple explicit water molecular dynamics simulations of the H4 tail peptide into the catalytic cleft of PARP1 indicate that two stable intermolecular salt bridges hold the peptide in an orientation that allows K16 ADP-ribosylation. Consistent with a functional cross-talk between ADP-ribosylation and other histone tail modifications, acetylation of H4K16 inhibits ADP-ribosylation by PARP1. Taken together, our computational and experimental results provide strong evidence that PARP1 modifies important regulatory lysines of the core histone tails.
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Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation
Timinszky, G., Till, S., Hassa, P. O., Hothorn, M., Kustatscher, G., Nijmeijer, B., Colombelli, J., Altmeyer, M., Stelzer, E. H. K., Scheffzek, K., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1664 · Cited by 416
Self-citation
Cited by
The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
Ray Chaudhuri, A., & Nussenzweig, A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.53 · Cited by 1,786
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681
“…PAR and ADP-ribose to reduce complexity using enzymes, such as snake venom phosphodiesterase (SVP), ARH3, PARG, or NUDIX hydrolases, is becoming a popular approach as a prelude to MS (Messner et al. 2010; Chapman et al. 2013; Sharifi et al. 2013; Daniels et al. 2014, 2015b; Martello et al. 2016).”
BackgroundDNA damage and its links to neurodegeneration
Madabhushi, R., Pan, L., & Tsai, L.-H. (2014) · Neuron · doi:10.1016/j.neuron.2014.06.034 · Cited by 654
Lukas, J., Lukas, C., & Bartek, J. (2011) · Nature Cell Biology · doi:10.1038/ncb2344 · Cited by 645
Serine ADP-ribosylation depends on HPF1
Bonfiglio, J. J., Fontana, P., Zhang, Q., Colby, T., Gibbs-Seymour, I., Atanassov, I., Bartlett, E., Zaja, R., Ahel, I., & Matic, I. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.01.003 · Cited by 352
Metadata
- Authors
- Messner, S., Altmeyer, M., Zhao, H., Pozivil, A., Roschitzki, B., Gehrig, P., Rutishauser, D., Huang, D., Caflisch, A., & Hottiger, M. O.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-06-04
- Volume
- 38
- Issue
- 19
- Pages
- 6350-6362
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W1974916823
- Cited by
- 264
- References
- 4
- FWCI
- 7.56
- Type
- journal article
- Language
- en
- Open access
- gold
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- Messner, S., Altmeyer, M., Zhao, H., Pozivil, A., Roschitzki, B., Gehrig, P., Rutishauser, D., Huang, D., Caflisch, A., & Hottiger, M. O. (2010). PARP1 ADP-ribosylates lysine residues of the core histone tails. Nucleic Acids Research. https://doi.org/10.1093/nar/gkq463
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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