| http://purl.uniprot.org/citations/34874266 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34874266 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34874266 | http://www.w3.org/2000/01/rdf-schema#comment | "Serine ADP-ribosylation (ADPr) is a DNA damage-induced post-translational modification catalyzed by the PARP1/2:HPF1 complex. As the list of PARP1/2:HPF1 substrates continues to expand, there is a need for technologies to prepare mono- and poly-ADP-ribosylated proteins for biochemical interrogation. Here, we investigate the unique peptide ADPr activities catalyzed by PARP1 in the absence and presence of HPF1. We then exploit these activities to develop a method that facilitates installation of ADP-ribose polymers onto peptides with precise control over chain length and modification site. Importantly, the enzymatically mono- and poly-ADP-ribosylated peptides are fully compatible with protein ligation technologies. This chemoenzymatic protein synthesis strategy was employed to assemble a series of full-length, ADP-ribosylated histones and show that ADPr at histone H2B serine 6 or histone H3 serine 10 converts nucleosomes into robust substrates for the chromatin remodeler ALC1. We found ALC1 preferentially remodels 'activated' substrates within heterogeneous mononucleosome populations and asymmetrically ADP-ribosylated dinucleosome substrates, and that nucleosome serine ADPr is sufficient to stimulate ALC1 activity in nuclear extracts. Our study identifies a biochemical function for nucleosome serine ADPr and describes a new, highly modular approach to explore the impact that site-specific serine mono- and poly-ADPr have on protein function."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.71502"xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.org/dc/terms/identifier | "doi:10.7554/elife.71502"xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Liszczak G."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Liszczak G."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Tashiro K."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Tashiro K."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Williams N.S."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Williams N.S."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Beckner R.L."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Beckner R.L."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Kilgore J.A."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Kilgore J.A."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Mohapatra J."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Mohapatra J."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Sierra J."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/author | "Sierra J."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/name | "Elife"xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/name | "Elife"xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/title | "Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling."xsd:string |
| http://purl.uniprot.org/citations/34874266 | http://purl.uniprot.org/core/title | "Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling."xsd:string |