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(A) A poly(U)-Cy3 oligo was ADP-ribosylated by PARP15cat and purified after <t>proteinase</t> <t>K</t> digest. Activity of different hydrolases was assessed by incubating the ADPr-RNA oligo with 1 µM of indicated hydrolases for 30 min at 37ºC. Reactions were resolved on urea-PAGE and in-gel fluorescence detected. (B) Oligonucleotides were ADP-ribosylated with ScARP and purified as in (A) and incubated with either 100 nM NADAR or TARG1 for 30 min at RT. After separation on urea-PAGE the gels were stained with SYBR Gold and analysed by in-gel fluorescence. (C) Oligonucleotides were ADP-ribosylated with PARP15cat and ADPr-ribosylhydrolase activity of 100 nM NADAR and TARG1 analysed as in (A). (D) ADPr-RNA-poly(U)-Cy3 was prepared using PARP15cat as in (B) and then incubated with indicated concentrations of TARG1, followed by urea-PAGE and in-gel fluorescence detection. (E) As in (D), with inclusion of TARG1 mutants at 50 nM concentration. (F) ADPr-poly(U)-Cy3 prepared as in (D) was incubated with indicated concentrations of TARG1 K84A mutant and detected as in (D). (G) Comparison of the protein surfaces of DarG (5m3e) and TARG1 (4j5r), highlighting the electrostatic surface potential. (H) Cartoon representation of TARG1 crystal structure (4j5r) with indicated residues contributing to the positively charged surface potentially involved in RNA binding. (I) Electrophoretic mobility shift assay with P-labelled pentaprobe RNAs. Purified pentaprobe 9 ( P-PP9) was incubated with the indicated amounts of TARG1 or TARG1 triple K50D/R86D/R126D mutant (KRR). Unbound RNA was separated from protein-bound RNA on native 7% polyacrylamide gels. Mobility shifts were analysed by autoradiography. (J) ADPr-poly(U)-Cy3 was prepared as in (A) prior to incubation with indicated amounts of TARG1 wild-type or K50D/R86D/R126D mutant (KRR). Reactions were separated using urea-PAGE and in-gel fluorescence was detected. (K) A model substrate protein, NPM1, was ADP-ribosylated using PARP10cat and radiolabelled NAD + . ADP-ribosylated proteins were incubated with TARG1 or the indicated mutants. Reactions were separated using SDS-PAGE, followed by Coomassie staining (CB) and detection of P by radiography.
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proteinase k treatment  (MedChemExpress)
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(A) A poly(U)-Cy3 oligo was ADP-ribosylated by PARP15cat and purified after <t>proteinase</t> <t>K</t> digest. Activity of different hydrolases was assessed by incubating the ADPr-RNA oligo with 1 µM of indicated hydrolases for 30 min at 37ºC. Reactions were resolved on urea-PAGE and in-gel fluorescence detected. (B) Oligonucleotides were ADP-ribosylated with ScARP and purified as in (A) and incubated with either 100 nM NADAR or TARG1 for 30 min at RT. After separation on urea-PAGE the gels were stained with SYBR Gold and analysed by in-gel fluorescence. (C) Oligonucleotides were ADP-ribosylated with PARP15cat and ADPr-ribosylhydrolase activity of 100 nM NADAR and TARG1 analysed as in (A). (D) ADPr-RNA-poly(U)-Cy3 was prepared using PARP15cat as in (B) and then incubated with indicated concentrations of TARG1, followed by urea-PAGE and in-gel fluorescence detection. (E) As in (D), with inclusion of TARG1 mutants at 50 nM concentration. (F) ADPr-poly(U)-Cy3 prepared as in (D) was incubated with indicated concentrations of TARG1 K84A mutant and detected as in (D). (G) Comparison of the protein surfaces of DarG (5m3e) and TARG1 (4j5r), highlighting the electrostatic surface potential. (H) Cartoon representation of TARG1 crystal structure (4j5r) with indicated residues contributing to the positively charged surface potentially involved in RNA binding. (I) Electrophoretic mobility shift assay with P-labelled pentaprobe RNAs. Purified pentaprobe 9 ( P-PP9) was incubated with the indicated amounts of TARG1 or TARG1 triple K50D/R86D/R126D mutant (KRR). Unbound RNA was separated from protein-bound RNA on native 7% polyacrylamide gels. Mobility shifts were analysed by autoradiography. (J) ADPr-poly(U)-Cy3 was prepared as in (A) prior to incubation with indicated amounts of TARG1 wild-type or K50D/R86D/R126D mutant (KRR). Reactions were separated using urea-PAGE and in-gel fluorescence was detected. (K) A model substrate protein, NPM1, was ADP-ribosylated using PARP10cat and radiolabelled NAD + . ADP-ribosylated proteins were incubated with TARG1 or the indicated mutants. Reactions were separated using SDS-PAGE, followed by Coomassie staining (CB) and detection of P by radiography.
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(A) A poly(U)-Cy3 oligo was ADP-ribosylated by PARP15cat and purified after <t>proteinase</t> <t>K</t> digest. Activity of different hydrolases was assessed by incubating the ADPr-RNA oligo with 1 µM of indicated hydrolases for 30 min at 37ºC. Reactions were resolved on urea-PAGE and in-gel fluorescence detected. (B) Oligonucleotides were ADP-ribosylated with ScARP and purified as in (A) and incubated with either 100 nM NADAR or TARG1 for 30 min at RT. After separation on urea-PAGE the gels were stained with SYBR Gold and analysed by in-gel fluorescence. (C) Oligonucleotides were ADP-ribosylated with PARP15cat and ADPr-ribosylhydrolase activity of 100 nM NADAR and TARG1 analysed as in (A). (D) ADPr-RNA-poly(U)-Cy3 was prepared using PARP15cat as in (B) and then incubated with indicated concentrations of TARG1, followed by urea-PAGE and in-gel fluorescence detection. (E) As in (D), with inclusion of TARG1 mutants at 50 nM concentration. (F) ADPr-poly(U)-Cy3 prepared as in (D) was incubated with indicated concentrations of TARG1 K84A mutant and detected as in (D). (G) Comparison of the protein surfaces of DarG (5m3e) and TARG1 (4j5r), highlighting the electrostatic surface potential. (H) Cartoon representation of TARG1 crystal structure (4j5r) with indicated residues contributing to the positively charged surface potentially involved in RNA binding. (I) Electrophoretic mobility shift assay with P-labelled pentaprobe RNAs. Purified pentaprobe 9 ( P-PP9) was incubated with the indicated amounts of TARG1 or TARG1 triple K50D/R86D/R126D mutant (KRR). Unbound RNA was separated from protein-bound RNA on native 7% polyacrylamide gels. Mobility shifts were analysed by autoradiography. (J) ADPr-poly(U)-Cy3 was prepared as in (A) prior to incubation with indicated amounts of TARG1 wild-type or K50D/R86D/R126D mutant (KRR). Reactions were separated using urea-PAGE and in-gel fluorescence was detected. (K) A model substrate protein, NPM1, was ADP-ribosylated using PARP10cat and radiolabelled NAD + . ADP-ribosylated proteins were incubated with TARG1 or the indicated mutants. Reactions were separated using SDS-PAGE, followed by Coomassie staining (CB) and detection of P by radiography.
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proteinase k treatment  (Vazyme Biotech Co)
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(A) A poly(U)-Cy3 oligo was ADP-ribosylated by PARP15cat and purified after <t>proteinase</t> <t>K</t> digest. Activity of different hydrolases was assessed by incubating the ADPr-RNA oligo with 1 µM of indicated hydrolases for 30 min at 37ºC. Reactions were resolved on urea-PAGE and in-gel fluorescence detected. (B) Oligonucleotides were ADP-ribosylated with ScARP and purified as in (A) and incubated with either 100 nM NADAR or TARG1 for 30 min at RT. After separation on urea-PAGE the gels were stained with SYBR Gold and analysed by in-gel fluorescence. (C) Oligonucleotides were ADP-ribosylated with PARP15cat and ADPr-ribosylhydrolase activity of 100 nM NADAR and TARG1 analysed as in (A). (D) ADPr-RNA-poly(U)-Cy3 was prepared using PARP15cat as in (B) and then incubated with indicated concentrations of TARG1, followed by urea-PAGE and in-gel fluorescence detection. (E) As in (D), with inclusion of TARG1 mutants at 50 nM concentration. (F) ADPr-poly(U)-Cy3 prepared as in (D) was incubated with indicated concentrations of TARG1 K84A mutant and detected as in (D). (G) Comparison of the protein surfaces of DarG (5m3e) and TARG1 (4j5r), highlighting the electrostatic surface potential. (H) Cartoon representation of TARG1 crystal structure (4j5r) with indicated residues contributing to the positively charged surface potentially involved in RNA binding. (I) Electrophoretic mobility shift assay with P-labelled pentaprobe RNAs. Purified pentaprobe 9 ( P-PP9) was incubated with the indicated amounts of TARG1 or TARG1 triple K50D/R86D/R126D mutant (KRR). Unbound RNA was separated from protein-bound RNA on native 7% polyacrylamide gels. Mobility shifts were analysed by autoradiography. (J) ADPr-poly(U)-Cy3 was prepared as in (A) prior to incubation with indicated amounts of TARG1 wild-type or K50D/R86D/R126D mutant (KRR). Reactions were separated using urea-PAGE and in-gel fluorescence was detected. (K) A model substrate protein, NPM1, was ADP-ribosylated using PARP10cat and radiolabelled NAD + . ADP-ribosylated proteins were incubated with TARG1 or the indicated mutants. Reactions were separated using SDS-PAGE, followed by Coomassie staining (CB) and detection of P by radiography.
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(A) A poly(U)-Cy3 oligo was ADP-ribosylated by PARP15cat and purified after <t>proteinase</t> <t>K</t> digest. Activity of different hydrolases was assessed by incubating the ADPr-RNA oligo with 1 µM of indicated hydrolases for 30 min at 37ºC. Reactions were resolved on urea-PAGE and in-gel fluorescence detected. (B) Oligonucleotides were ADP-ribosylated with ScARP and purified as in (A) and incubated with either 100 nM NADAR or TARG1 for 30 min at RT. After separation on urea-PAGE the gels were stained with SYBR Gold and analysed by in-gel fluorescence. (C) Oligonucleotides were ADP-ribosylated with PARP15cat and ADPr-ribosylhydrolase activity of 100 nM NADAR and TARG1 analysed as in (A). (D) ADPr-RNA-poly(U)-Cy3 was prepared using PARP15cat as in (B) and then incubated with indicated concentrations of TARG1, followed by urea-PAGE and in-gel fluorescence detection. (E) As in (D), with inclusion of TARG1 mutants at 50 nM concentration. (F) ADPr-poly(U)-Cy3 prepared as in (D) was incubated with indicated concentrations of TARG1 K84A mutant and detected as in (D). (G) Comparison of the protein surfaces of DarG (5m3e) and TARG1 (4j5r), highlighting the electrostatic surface potential. (H) Cartoon representation of TARG1 crystal structure (4j5r) with indicated residues contributing to the positively charged surface potentially involved in RNA binding. (I) Electrophoretic mobility shift assay with P-labelled pentaprobe RNAs. Purified pentaprobe 9 ( P-PP9) was incubated with the indicated amounts of TARG1 or TARG1 triple K50D/R86D/R126D mutant (KRR). Unbound RNA was separated from protein-bound RNA on native 7% polyacrylamide gels. Mobility shifts were analysed by autoradiography. (J) ADPr-poly(U)-Cy3 was prepared as in (A) prior to incubation with indicated amounts of TARG1 wild-type or K50D/R86D/R126D mutant (KRR). Reactions were separated using urea-PAGE and in-gel fluorescence was detected. (K) A model substrate protein, NPM1, was ADP-ribosylated using PARP10cat and radiolabelled NAD + . ADP-ribosylated proteins were incubated with TARG1 or the indicated mutants. Reactions were separated using SDS-PAGE, followed by Coomassie staining (CB) and detection of P by radiography.
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(A) A poly(U)-Cy3 oligo was ADP-ribosylated by PARP15cat and purified after proteinase K digest. Activity of different hydrolases was assessed by incubating the ADPr-RNA oligo with 1 µM of indicated hydrolases for 30 min at 37ºC. Reactions were resolved on urea-PAGE and in-gel fluorescence detected. (B) Oligonucleotides were ADP-ribosylated with ScARP and purified as in (A) and incubated with either 100 nM NADAR or TARG1 for 30 min at RT. After separation on urea-PAGE the gels were stained with SYBR Gold and analysed by in-gel fluorescence. (C) Oligonucleotides were ADP-ribosylated with PARP15cat and ADPr-ribosylhydrolase activity of 100 nM NADAR and TARG1 analysed as in (A). (D) ADPr-RNA-poly(U)-Cy3 was prepared using PARP15cat as in (B) and then incubated with indicated concentrations of TARG1, followed by urea-PAGE and in-gel fluorescence detection. (E) As in (D), with inclusion of TARG1 mutants at 50 nM concentration. (F) ADPr-poly(U)-Cy3 prepared as in (D) was incubated with indicated concentrations of TARG1 K84A mutant and detected as in (D). (G) Comparison of the protein surfaces of DarG (5m3e) and TARG1 (4j5r), highlighting the electrostatic surface potential. (H) Cartoon representation of TARG1 crystal structure (4j5r) with indicated residues contributing to the positively charged surface potentially involved in RNA binding. (I) Electrophoretic mobility shift assay with P-labelled pentaprobe RNAs. Purified pentaprobe 9 ( P-PP9) was incubated with the indicated amounts of TARG1 or TARG1 triple K50D/R86D/R126D mutant (KRR). Unbound RNA was separated from protein-bound RNA on native 7% polyacrylamide gels. Mobility shifts were analysed by autoradiography. (J) ADPr-poly(U)-Cy3 was prepared as in (A) prior to incubation with indicated amounts of TARG1 wild-type or K50D/R86D/R126D mutant (KRR). Reactions were separated using urea-PAGE and in-gel fluorescence was detected. (K) A model substrate protein, NPM1, was ADP-ribosylated using PARP10cat and radiolabelled NAD + . ADP-ribosylated proteins were incubated with TARG1 or the indicated mutants. Reactions were separated using SDS-PAGE, followed by Coomassie staining (CB) and detection of P by radiography.

Journal: bioRxiv

Article Title: Human PARPs modify RNA nucleobases in vitro and in cells

doi: 10.64898/2026.03.31.715305

Figure Lengend Snippet: (A) A poly(U)-Cy3 oligo was ADP-ribosylated by PARP15cat and purified after proteinase K digest. Activity of different hydrolases was assessed by incubating the ADPr-RNA oligo with 1 µM of indicated hydrolases for 30 min at 37ºC. Reactions were resolved on urea-PAGE and in-gel fluorescence detected. (B) Oligonucleotides were ADP-ribosylated with ScARP and purified as in (A) and incubated with either 100 nM NADAR or TARG1 for 30 min at RT. After separation on urea-PAGE the gels were stained with SYBR Gold and analysed by in-gel fluorescence. (C) Oligonucleotides were ADP-ribosylated with PARP15cat and ADPr-ribosylhydrolase activity of 100 nM NADAR and TARG1 analysed as in (A). (D) ADPr-RNA-poly(U)-Cy3 was prepared using PARP15cat as in (B) and then incubated with indicated concentrations of TARG1, followed by urea-PAGE and in-gel fluorescence detection. (E) As in (D), with inclusion of TARG1 mutants at 50 nM concentration. (F) ADPr-poly(U)-Cy3 prepared as in (D) was incubated with indicated concentrations of TARG1 K84A mutant and detected as in (D). (G) Comparison of the protein surfaces of DarG (5m3e) and TARG1 (4j5r), highlighting the electrostatic surface potential. (H) Cartoon representation of TARG1 crystal structure (4j5r) with indicated residues contributing to the positively charged surface potentially involved in RNA binding. (I) Electrophoretic mobility shift assay with P-labelled pentaprobe RNAs. Purified pentaprobe 9 ( P-PP9) was incubated with the indicated amounts of TARG1 or TARG1 triple K50D/R86D/R126D mutant (KRR). Unbound RNA was separated from protein-bound RNA on native 7% polyacrylamide gels. Mobility shifts were analysed by autoradiography. (J) ADPr-poly(U)-Cy3 was prepared as in (A) prior to incubation with indicated amounts of TARG1 wild-type or K50D/R86D/R126D mutant (KRR). Reactions were separated using urea-PAGE and in-gel fluorescence was detected. (K) A model substrate protein, NPM1, was ADP-ribosylated using PARP10cat and radiolabelled NAD + . ADP-ribosylated proteins were incubated with TARG1 or the indicated mutants. Reactions were separated using SDS-PAGE, followed by Coomassie staining (CB) and detection of P by radiography.

Article Snippet: After proteinase K treatment and purification ADPr-RNA Gluc was enriched using Anti-PAR/MAR (E6F6A0, Cell Signalling Technology (CST)) coupled to protein A/G magnetic agarose beads (Pierce).

Techniques: Purification, Activity Assay, Fluorescence, Incubation, Staining, Concentration Assay, Mutagenesis, Comparison, RNA Binding Assay, Electrophoretic Mobility Shift Assay, Autoradiography, SDS Page