Interplay of histone marks with serine ADP-ribosylation
Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1). In addition to numerous other targets, core histone tails are primary acceptors of Ser-ADPr in the DNA damage r...
| প্রধান লেখক: | , , , , , , |
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| বিন্যাস: | Journal article |
| ভাষা: | English |
| প্রকাশিত: |
Cell Press
2018
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| _version_ | 1826293697729265664 |
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| author | Bartlett, E Bonfiglio, J Prokhorova, E Colby, T Zobel, F Ahel, I Matic, I |
| author_facet | Bartlett, E Bonfiglio, J Prokhorova, E Colby, T Zobel, F Ahel, I Matic, I |
| author_sort | Bartlett, E |
| collection | OXFORD |
| description | Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1). In addition to numerous other targets, core histone tails are primary acceptors of Ser-ADPr in the DNA damage response. Here, we show that specific canonical histone marks interfere with Ser-ADPr of neighboring residues and vice versa. Most notably, acetylation, but not methylation of H3K9, is mutually exclusive with ADPr of H3S10 in vitro and in vivo. We also broaden the O-linked ADPr spectrum by providing evidence for tyrosine ADPr on HPF1 and other proteins. Finally, we facilitate wider investigations into the interplay of histone marks with Ser-ADPr by introducing a simple approach for profiling posttranslationally modified peptides. Our findings implicate Ser-ADPr as a dynamic addition to the complex interplay of modifications that shape the histone code. |
| first_indexed | 2024-03-07T03:34:09Z |
| format | Journal article |
| id | oxford-uuid:bbbca2e9-0230-4f52-81d4-ede8b84c33c0 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:34:09Z |
| publishDate | 2018 |
| publisher | Cell Press |
| record_format | dspace |
| spelling | oxford-uuid:bbbca2e9-0230-4f52-81d4-ede8b84c33c02022-03-27T05:19:04ZInterplay of histone marks with serine ADP-ribosylationJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bbbca2e9-0230-4f52-81d4-ede8b84c33c0EnglishSymplectic Elements at OxfordCell Press2018Bartlett, EBonfiglio, JProkhorova, EColby, TZobel, FAhel, IMatic, ISerine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1). In addition to numerous other targets, core histone tails are primary acceptors of Ser-ADPr in the DNA damage response. Here, we show that specific canonical histone marks interfere with Ser-ADPr of neighboring residues and vice versa. Most notably, acetylation, but not methylation of H3K9, is mutually exclusive with ADPr of H3S10 in vitro and in vivo. We also broaden the O-linked ADPr spectrum by providing evidence for tyrosine ADPr on HPF1 and other proteins. Finally, we facilitate wider investigations into the interplay of histone marks with Ser-ADPr by introducing a simple approach for profiling posttranslationally modified peptides. Our findings implicate Ser-ADPr as a dynamic addition to the complex interplay of modifications that shape the histone code. |
| spellingShingle | Bartlett, E Bonfiglio, J Prokhorova, E Colby, T Zobel, F Ahel, I Matic, I Interplay of histone marks with serine ADP-ribosylation |
| title | Interplay of histone marks with serine ADP-ribosylation |
| title_full | Interplay of histone marks with serine ADP-ribosylation |
| title_fullStr | Interplay of histone marks with serine ADP-ribosylation |
| title_full_unstemmed | Interplay of histone marks with serine ADP-ribosylation |
| title_short | Interplay of histone marks with serine ADP-ribosylation |
| title_sort | interplay of histone marks with serine adp ribosylation |
| work_keys_str_mv | AT bartlette interplayofhistonemarkswithserineadpribosylation AT bonfiglioj interplayofhistonemarkswithserineadpribosylation AT prokhorovae interplayofhistonemarkswithserineadpribosylation AT colbyt interplayofhistonemarkswithserineadpribosylation AT zobelf interplayofhistonemarkswithserineadpribosylation AT aheli interplayofhistonemarkswithserineadpribosylation AT matici interplayofhistonemarkswithserineadpribosylation |