Unknown

Dataset Information

0

Genetically Encoded Fluorescent Sensor for Poly-ADP-Ribose.

ABSTRACT: Poly-(ADP-ribosyl)-ation (PARylation) is a reversible post-translational modification of proteins and DNA that plays an important role in various cellular processes such as DNA damage response, replication, transcription, and cell death. Here we designed a fully genetically encoded fluorescent sensor for poly-(ADP-ribose) (PAR) based on Förster resonance energy transfer (FRET). The WWE domain, which recognizes iso-ADP-ribose internal PAR-specific structural unit, was used as a PAR-targeting module. The sensor consisted of cyan Turquoise2 and yellow Venus fluorescent proteins, each in fusion with the WWE domain of RNF146 E3 ubiquitin ligase protein. This bipartite sensor named sPARroW (sensor for PAR relying on WWE) enabled monitoring of PAR accumulation and depletion in live mammalian cells in response to different stimuli, namely hydrogen peroxide treatment, UV irradiation and hyperthermia.

SUBMITTER: Serebrovskaya EO 

PROVIDER: S-EPMC7404130 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Poly-(ADP-ribosyl)-ation (PARylation) is a reversible post-translational modification of proteins and DNA that plays an important role in various cellular processes such as DNA damage response, replication, transcription, and cell death. Here we designed a fully genetically encoded fluorescent sensor for poly-(ADP-ribose) (PAR) based on Förster resonance energy transfer (FRET). The WWE domain, which recognizes iso-ADP-ribose internal PAR-specific structural unit, was used as a PAR-targeting modu  ...[more]

Similar Datasets

Unknown A genetically encoded fluorescent reporter of ATP:ADP ratio.
| S-EPMC2633436 | biostudies-literature
Unknown A genetically encoded fluorescent sensor of ERK activity.
| S-EPMC2614750 | biostudies-literature
Unknown MagFRET: the first genetically encoded fluorescent Mg2+ sensor.
| S-EPMC3846734 | biostudies-literature
Unknown Detection of Osmotic Shock-Induced Extracellular Nucleotide Release with a Genetically Encoded Fluorescent Sensor of ADP and ATP.
| S-EPMC6695626 | biostudies-literature
Unknown Imaging extracellular ATP with a genetically-encoded, ratiometric fluorescent sensor.
| S-EPMC5679667 | biostudies-literature
Unknown Visualizing myosin-actin interaction with a genetically-encoded fluorescent strain sensor.
| S-EPMC2579347 | biostudies-literature
Unknown Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes.
| S-EPMC2602769 | biostudies-literature
Unknown Genetically encoded fluorescent tags.
| S-EPMC5385933 | biostudies-literature
Unknown Synthesis of dimeric ADP-ribose and its structure with human poly(ADP-ribose) glycohydrolase.
| S-EPMC6089346 | biostudies-literature
Unknown ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose).
| S-EPMC3351285 | biostudies-literature