Progress and outlook in studying the substrate specificities of PARPs and related enzymes.
ADP-ribosylation
DNA repair
HPF1
PARP
PARP1
PARP9
enzymatic catalysis
poly(ADP-ribosylation)
post-translational modification
specificity
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
04 2021
04 2021
Historique:
revised:
13
07
2020
received:
30
04
2020
accepted:
08
08
2020
pubmed:
14
8
2020
medline:
21
7
2021
entrez:
14
8
2020
Statut:
ppublish
Résumé
Despite decades of research on ADP-ribosyltransferases (ARTs) from the poly(ADP-ribose) polymerase (PARP) family, one key aspect of these enzymes - their substrate specificity - has remained unclear. Here, we briefly discuss the history of this area and, more extensively, the recent breakthroughs, including the identification of protein serine residues as a major substrate of PARP1 and PARP2 in human cells and of cysteine and tyrosine as potential targets of specific PARPs. On the molecular level, the modification of serine residues requires a composite active site formed by PARP1 or PARP2 together with a specificity-determining factor, HPF1; this represents a new paradigm not only for PARPs but generally for post-translational modification (PTM) catalysis. Additionally, we discuss the identification of DNA as a substrate of PARP1, PARP2 and PARP3, and some bacterial ARTs and the discovery of noncanonical RNA capping by several PARP family members. Together, these recent findings shed new light on PARP-mediated catalysis and caution to 'expect the unexpected' when it comes to further potential substrates.
Substances chimiques
Carrier Proteins
0
Cell Cycle Proteins
0
HPF1 protein, human
0
Nuclear Proteins
0
RNA Caps
0
DNA
9007-49-2
ADP Ribose Transferases
EC 2.4.2.-
PARP2 protein, human
EC 2.4.2.30
PARP3 protein, human
EC 2.4.2.30
Poly (ADP-Ribose) Polymerase-1
EC 2.4.2.30
Poly(ADP-ribose) Polymerases
EC 2.4.2.30
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2131-2142Subventions
Organisme : Wellcome Trust
ID : 101794
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R007195/1
Pays : United Kingdom
Informations de copyright
© 2020 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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