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  Serine is the major residue for ADP-ribosylation upon DNA damage

Palazzo, L., Leidecker, O., Prokhorova, E., Dauben, H., Matić, I., & Ahel, I. (2018). Serine is the major residue for ADP-ribosylation upon DNA damage. Elife, 7. doi:10.7554/eLife.34334.

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Palazzo, L., Author
Leidecker, O.1, Author           
Prokhorova, E., Author
Dauben, H.1, Author           
Matić, I.1, Author           
Ahel, I., Author
Affiliations:
1Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942299              

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Free keywords: biochemistry chemical biology human
 Abstract: PARPs are a family of enzymes that synthesise ADP-ribosylation (ADPr), a reversible modification of proteins that regulates many different cellular processes. Several mammalian PARPs are known to regulate the DNA damage response, but it is not clear which amino acids in proteins are the primary ADPr targets. Previously we reported that ARH3 reverses the newly discovered type of ADPr (ADPr on serine residues; Ser-ADPr) and developed tools to analyse this modification (Fontana et al, 2017). Here we show that Ser-ADPr represents the major fraction of ADPr synthesised after DNA damage in mammalian cells and that globally Ser-ADPr is dependent on HPF1, PARP1 and ARH3. In the absence of HPF1, glutamate/aspartate become the main target residues for ADPr. Furthermore, we describe a method for site-specific validation of serine ADP-ribosylated substrates in cells. Our study establishes serine as the primary form of ADPr in DNA damage signalling.

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 Dates: 2018-02-262018
 Publication Status: Issued
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 Identifiers: Other: 29480802
DOI: 10.7554/eLife.34334
ISSN: 2050-084X (Electronic)2050-084X (Linking)
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Title: Elife
Source Genre: Journal
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Pages: - Volume / Issue: 7 Sequence Number: - Start / End Page: - Identifier: -