Journal
FRONTIERS IN PLANT SCIENCE
Volume 9, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fpls.2018.01581
Keywords
Poly(ADP-Ribose) Polymerase; PARP2; nuclear localization sequence; nucleo-cytoplasmic transport; importin-alpha; Arabidopsis thaliana
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Funding
- German Research Foundation (DFG) [WI 3670/2-1]
- FU Berlin Dahlem Centre of Plant Sciences
- Freie Universitat Berlin - China Scholarship Council (FUB-CSC)
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Proteins of the PolyADP-Ribose) Polymerase PARP) family modify target proteins by covalent attachment of ADP-ribose moieties onto amino acid side chains. In Arabidopsis, PARP proteins contribute to repair of DNA lesions and modulate plant responses to various abiotic and biotic stressors. Arabidopsis PARP1 and PARP2 are nuclear proteins and given that their molecular weights exceed the diffusion limit of nuclear pore complexes, an active import mechanism into the nucleus is likely. Here we use confocal microscopy of fluorescent protein-tagged Arabidopsis PARP2 and PARP2 deletion constructs in combination with site-directed mutagenesis to identify a nuclear localization sequence in PARP2 that is required for nuclear import. We report that in co-immunoprecipitation assays PARP2 interacts with several isoforms of the importin-alpha group of nuclear transport adapters and that PARP2 binding to IMPORTIN-alpha 2 is mediated by the identified nuclear localization sequence. Our results demonstrate that PARP2 is a cargo protein of the canonical importin-alpha/beta nuclear import pathway.
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