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Fan Z, Li J, Liu T, Zhang Z, Qin W, Qian X. A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome. The Analyst 2021 146(4) 33465208
Abstract:
RNA-protein interactions play important roles in almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation. Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs). However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task. In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling. Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis. Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs. Interestingly, ∼25% RBPs modified by two PTMs were found to be related to multiple metabolism pathways. This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs. We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
O-GlcNAc proteins:
NACAM, SAP18, PLOD2, NOP56, DDX3X, PLXB2, RRP8, SERA, PSMD3, MCA3, PRPF3, TPD54, TIM44, ACTN4, ACSL4, PLOD3, IF2P, ZC11A, SC22B, PR40A, MPPB, CSDE1, U520, NU155, EIF3G, SPF27, RL1D1, CLPX, RTN3, LC7L3, VAPB, SMC2, AP2A1, WIZ, BAG2, TOM40, ACL6A, EGFR, LMNA, TFR1, FRIH, RPN1, RPN2, ITB1, SYEP, HNRPC, SRPRA, VIME, GNAI3, ANXA5, LAMP1, ACADM, TOP1, TOP2A, PABP1, ADT3, TPR, EF2, PDIA4, FPPS, ENPL, ALDR, NDKA, RS2, UBF1, ARF4, NUCL, RAB6A, PSB1, FLNA, SDHB, UBA1, NDKB, ITA6, SFPQ, AT2B4, THIL, RS12, PSA4, SYVC, 1433T, MAP4, PSA5, PSB4, NDUS1, ECHM, KCY, AMRP, SDHA, METK2, CPSM, PUR9, HNRH1, 1433S, STIP1, P5CR1, MCM4, HSP74, CTNA1, MYH9, DEK, RL4, SPB5, NUP62, RBMX, TCPZ, ECE1, PRS6B, KI67, RAGP1, ATRX, SYQ, LMAN1, NASP, FAS, AL7A1, SYSC, MCM2, ACADV, NU153, RBP2, DNLI3, MRE11, CPT1A, F10A1, TCPD, RAB7A, IDH3G, HCFC1, DHB4, HDGF, ROA3, 6PGD, NUP98, ACLY, TCP4, SYYC, UBP14, SNAA, IF5, TERA, DSRAD, TPD52, EIF3B, NU107, EPIPL, SC61B, SRP54, B2MG, SMD2, RL23A, YBOX1, NOP14, IF4G2, GTF2I, NUCB2, RT22, HMGN5, RBM10, TFAM, CLH1, SPTB2, SET, CAP1, EXOSX, EWS, ODO1, RL18A, NUCB1, M2OM, LMNB2, SRS11, CALD1, RL18, C1QBP, CKAP4, KHDR1, DHX9, GOGA2, SSRP1, AHNK, AIMP1, ILF3, SRSF5, SRSF6, TIF1B, TCOF, PICAL, SNW1, TRI29, EIF3A, MLEC, CAPR1, SMC1A, RRP1B, GANAB, NUMA1, U5S1, RRS1, ACOX1, PLEC, RNPS1, PUM3, RB11B, SEPT7, DDB1, CDC37, SRSF7, PCKGM, HNRL2, INF2, PDS5A, PREP, RRP12, TOIP1, HP1B3, RBM26, BRE1A, CDKAL, PRP8, ZC3HE, QSOX2, IKIP, TM10C, EIF3M, PABP2, KTN1, CAND1, THOC6, P66A, MISP, CCAR1, PELP1, NDUF2, RM50, PAF1, TXND5, TOIP2, THOC2, TM263, NU133, PDC6I, SCFD1, LMO7, ELYS, RT27, HS105, NU205, RAD50, SMRC1, TNPO1, FUBP1, P5CR2, DNJA3, PTCD3, DDX27, EFGM, IWS1, NIBA2, YMEL1, PSMD1, EIF3C, ROAA, CMS1, MBB1A, GNL3, PDIP3, PININ, ACAD9, SFXN1, CYBP, RM47, RTN4, DDX21, AAAS, CARF, AATF, BCLF1, MYOF, SYLC, NXF1, SEC63, LIMA1, SEPT9, KAD3, RCOR1, ACINU, TMCO1, PPIE, PA2G4, RUVB2, TR150, RT23, CHTOP, TLN1, HYOU1, SAM50, SP16H, UTP18, SRPRB
Species: Homo sapiens
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Nandi A, Sprung R, Barma DK, Zhao Y, Kim SC, Falck JR, Zhao Y. Global identification of O-GlcNAc-modified proteins. Analytical chemistry 2006 78(2) 16408927
Abstract:
The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins. The functions and subproteome of O-GlcNAc modification remain largely undefined. Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins. The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies. Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation. Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
Species: Homo sapiens
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