The rise and fall of poly(ADP-ribose): An enzymatic perspective

John M. Pascal; Tom Ellenberger

doi:10.1016/j.dnarep.2015.04.008

The rise and fall of poly(ADP-ribose): An enzymatic perspective

John M. Pascal
, Tom Ellenberger

Department of Biochemistry & Molecular Biophysics

Research output: Contribution to journal › Article › peer-review

88 Scopus citations

Abstract

Human cells respond to DNA damage with an acute and transient burst in production of poly(ADP-ribose), a posttranslational modification that expedites damage repair and plays a pivotal role in cell fate decisions. Poly(ADP-ribose) polymerases (PARPs) and glycohydrolase (PARG) are the key set of enzymes that orchestrate the rise and fall in cellular levels of poly(ADP-ribose). In this perspective, we focus on recent structural and mechanistic insights into the enzymes involved in poly(ADP-ribose) production and turnover, and we highlight important questions that remain to be answered.

Original language	English
Pages (from-to)	10-16
Number of pages	7
Journal	DNA Repair
Volume	32
DOIs	https://doi.org/10.1016/j.dnarep.2015.04.008
State	Published - Aug 1 2015

Keywords

ADP-ribose
DNA damage response
MARG
PARG
PARP
Poly(ADP-ribose)

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10.1016/j.dnarep.2015.04.008

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title = "The rise and fall of poly(ADP-ribose): An enzymatic perspective",

abstract = "Human cells respond to DNA damage with an acute and transient burst in production of poly(ADP-ribose), a posttranslational modification that expedites damage repair and plays a pivotal role in cell fate decisions. Poly(ADP-ribose) polymerases (PARPs) and glycohydrolase (PARG) are the key set of enzymes that orchestrate the rise and fall in cellular levels of poly(ADP-ribose). In this perspective, we focus on recent structural and mechanistic insights into the enzymes involved in poly(ADP-ribose) production and turnover, and we highlight important questions that remain to be answered.",

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AU - Ellenberger, Tom

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N2 - Human cells respond to DNA damage with an acute and transient burst in production of poly(ADP-ribose), a posttranslational modification that expedites damage repair and plays a pivotal role in cell fate decisions. Poly(ADP-ribose) polymerases (PARPs) and glycohydrolase (PARG) are the key set of enzymes that orchestrate the rise and fall in cellular levels of poly(ADP-ribose). In this perspective, we focus on recent structural and mechanistic insights into the enzymes involved in poly(ADP-ribose) production and turnover, and we highlight important questions that remain to be answered.

AB - Human cells respond to DNA damage with an acute and transient burst in production of poly(ADP-ribose), a posttranslational modification that expedites damage repair and plays a pivotal role in cell fate decisions. Poly(ADP-ribose) polymerases (PARPs) and glycohydrolase (PARG) are the key set of enzymes that orchestrate the rise and fall in cellular levels of poly(ADP-ribose). In this perspective, we focus on recent structural and mechanistic insights into the enzymes involved in poly(ADP-ribose) production and turnover, and we highlight important questions that remain to be answered.

KW - ADP-ribose

KW - DNA damage response

KW - MARG

KW - PARG

KW - PARP

KW - Poly(ADP-ribose)

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VL - 32

SP - 10

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JO - DNA Repair

JF - DNA Repair

ER -

The rise and fall of poly(ADP-ribose): An enzymatic perspective

Abstract

Keywords

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