Abstract

Poly(ADP-ribosyl)ation is a rapid and transient post-translational protein modification that was described first in mammalian cells. Activated by the sensing of DNA strand breaks, poly(ADP-ribose)polymerase1 (PARP1) transfers ADP-ribose units onto itself and other target proteins using NAD+ as a substrate. Subsequently, DNA damage responses and other cellular responses are initiated. In plants, poly(ADP-ribose) polymerases (PARPs) have also been implicated in responses to DNA damage. The Arabidopsis genome contains three canonical PARP genes, the nomenclature of which has been uncoordinated in the past. Albeit assumptions concerning the function and roles of PARP proteins in planta have often been inferred from homology and structural conservation between plant PARPs and their mammalian counterparts, plant-specific roles have become apparent. In particular, PARPs have been linked to stress responses of plants. A negative role under abiotic stress has been inferred from studies in which a genetic or, more commonly, pharmacological inhibition of PARP activity improved the performance of stressed plants; in response to pathogen-associated molecular patterns, a positive role has been suggested. However, reports have been inconsistent, and the effects of PARP inhibitors appear to be more robust than the genetic abolition of PARP gene expression, indicating the presence of alternative targets of those drugs. Collectively, recent evidence suggests a conditionality of stress-related phenotypes of parp mutants and calls for a reconsideration of PARP inhibitor studies on plants. This review critically summarizes our current understanding of poly(ADP-ribosylation) and PARP proteins in plants, highlighting similarities and differences to human PARPs, areas of controversy, and requirements for future studies.

Highlights

  • Poly(ADP-ribosyl)ation describes the rapid and transient posttranslational transfer of negatively charged ADP-ribose molecules onto proteins

  • The amino acids modified by poly(ADP-ribosyl)ation in the target proteins are predominantly glutamic acid and aspartic acid; modification is performed via ester linkage [26,27,28]

  • The AtPARP2 cDNA was identified due to its 62% similarity to the catalytic domain of human PARP1 during experiments carried out to identify Arabidopsis proteins that allow yeast cells to grow under stress conditions

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Summary

Introduction

Poly(ADP-ribosyl)ation describes the rapid and transient posttranslational transfer of negatively charged ADP-ribose molecules onto proteins. Several poly(ADP-ribosyl)ation site-containing proteins and poly(ADP-ribose) binding motif-containing proteins have been identified acting as poly(ADP-ribose) readers translating the poly(ADP-ribose) signal into cellular responses [8,9]. The modification of serine residues of target proteins by O-glycosidic bonds has been shown [29]; the enzymatic modification of lysine residues is currently a matter of debate [27,28]. In contrast to their mammalian counterparts, less is known about the functions of plant poly(ADP-ribose)polymerases. We will focus on plant-specific roles, such as in seeds, and in the determination of stress resistance by those proteins, which is currently a matter of controversy

PARPs Constitute a Heterogeneous Protein Family in Humans
Plant PARPs Play a Role in DNA Damage Response and Genome Integrity
PARP1 and PARP2 Are Actors in Various DNA Damage Response Pathways in Plants
PARP3 Is a Core Component of Genome Integrity in Seeds
Non-Canonical PARP Domain Proteins Act in Plant Stress Responses
Potential Off-Target Effects of PARP Inhibitors
Findings
PARPs Under Stress—Concluding Remarks and Future Perspectives
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