Project description:The protein PURA binds to DNA and RNA and has been suggested to be implicated in different cellular functions. Here, we show that PURA predominantly resides in the cytoplasm, where it binds to a large set of transcripts.
Project description:The protein PURA binds to DNA and RNA and has been suggested to be implicated in different cellular functions. Here, we show that PURA predominantly resides in the cytoplasm, where it binds to a large set of transcripts.
Project description:The protein PURA binds to DNA and RNA and has been suggested to be implicated in different cellular functions. Here, we show that PURA predominantly resides in the cytoplasm, where it binds to a large set of transcripts.
Project description:The protein PURA binds to DNA and RNA and has been suggested to be implicated in different cellular functions. Here, we show that PURA predominantly resides in the cytoplasm, where it binds to a large set of transcripts.
Project description:HeLa cells were cultured in DMEM, supplemented with 10% (v/v) FCS and penicillin/streptomycin under 5% CO2 at 37°C. For iCLIP, HeLa cells expressing eIF4A3-GFP or PTB-GFP were induced with doxycycline to adjust the level of recombinant protein to the level of the endogenous counterpart and irradiated with 150 mJ/cm2 UV light (254 nm). The iCLIP cDNA libraries for eIF4A3 and PTB were sequenced with 50 bp on an Illumina HiSeq instrument.
Project description:Here, we show that PURA predominantly resides in the cytoplasm, where it binds to a large set of transcripts. Many of these transcripts change abundance in response to PURA depletion, in parts reflected in altered protein expression levels. A closer inspection of the regulated proteins indicates a role of PURA in immune responses, mitochondrial function, autophagy and processing (P)-body activity.