Serine is a new target residue for endogenous ADP-ribosylation on histones

ADP-ribosylation (ADPr) is a biologically and clinically important post-translational modification, but little is known about the amino acids it targets on cellular proteins. Here we present a proteomic approach for direct in vivo identification and quantification of ADPr sites on histones. We have...

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Autores principales: Leidecker, Orsolya, Bonfiglio, Juan José, Colby, Thomas, Zhang, Qi, Atanassov, Ilian, Zaja, Roko, Palazzo, Luca, Stockum, Anna, Ahel, Ivan, Matic, Ivan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5113755/
https://www.ncbi.nlm.nih.gov/pubmed/27723750
http://dx.doi.org/10.1038/nchembio.2180
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author Leidecker, Orsolya
Bonfiglio, Juan José
Colby, Thomas
Zhang, Qi
Atanassov, Ilian
Zaja, Roko
Palazzo, Luca
Stockum, Anna
Ahel, Ivan
Matic, Ivan
author_facet Leidecker, Orsolya
Bonfiglio, Juan José
Colby, Thomas
Zhang, Qi
Atanassov, Ilian
Zaja, Roko
Palazzo, Luca
Stockum, Anna
Ahel, Ivan
Matic, Ivan
author_sort Leidecker, Orsolya
collection PubMed
description ADP-ribosylation (ADPr) is a biologically and clinically important post-translational modification, but little is known about the amino acids it targets on cellular proteins. Here we present a proteomic approach for direct in vivo identification and quantification of ADPr sites on histones. We have identified 12 unique ADPr sites in human osteosarcoma cells and report serine ADPr as a new type of histone mark that responds to DNA damage.
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spelling pubmed-51137552017-04-10 Serine is a new target residue for endogenous ADP-ribosylation on histones Leidecker, Orsolya Bonfiglio, Juan José Colby, Thomas Zhang, Qi Atanassov, Ilian Zaja, Roko Palazzo, Luca Stockum, Anna Ahel, Ivan Matic, Ivan Nat Chem Biol Article ADP-ribosylation (ADPr) is a biologically and clinically important post-translational modification, but little is known about the amino acids it targets on cellular proteins. Here we present a proteomic approach for direct in vivo identification and quantification of ADPr sites on histones. We have identified 12 unique ADPr sites in human osteosarcoma cells and report serine ADPr as a new type of histone mark that responds to DNA damage. 2016-10-10 2016-12 /pmc/articles/PMC5113755/ /pubmed/27723750 http://dx.doi.org/10.1038/nchembio.2180 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Leidecker, Orsolya
Bonfiglio, Juan José
Colby, Thomas
Zhang, Qi
Atanassov, Ilian
Zaja, Roko
Palazzo, Luca
Stockum, Anna
Ahel, Ivan
Matic, Ivan
Serine is a new target residue for endogenous ADP-ribosylation on histones
title Serine is a new target residue for endogenous ADP-ribosylation on histones
title_full Serine is a new target residue for endogenous ADP-ribosylation on histones
title_fullStr Serine is a new target residue for endogenous ADP-ribosylation on histones
title_full_unstemmed Serine is a new target residue for endogenous ADP-ribosylation on histones
title_short Serine is a new target residue for endogenous ADP-ribosylation on histones
title_sort serine is a new target residue for endogenous adp-ribosylation on histones
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5113755/
https://www.ncbi.nlm.nih.gov/pubmed/27723750
http://dx.doi.org/10.1038/nchembio.2180
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