053C YGL253W YBR196C YGR240C YMR205C RBP2GO
053C YGL253W YBR196C YGR240C YMR205C RBP2GO (score) 4/11 (27.3) 4/11 (26.4) 3/11 (30.five) 4/11 (24.5) 5/11 (35) Target, motif ReferenceOwn transcript (autoregulation) AU-rich components, 3 UTRs, coding sequence of, e.g., glycolysis-related transcripts, noncoding RNAs (mRNA localization to G-bodies) Noncoding RNAs and coding sequences, pyrimidine-rich motifs (mRNA localization to Gbodies)Scherrer et al. 2010 (RIPChip) Fuller et al. 2020 (PARCLIP-seq)Fructose-bisphosphate aldolase (fructose-1,6-bisphosphate)FBAYKL060C6/11 (35.9)Fuller et al. 2020 (PARCLIP-seq)Glyceraldehyde-3- phosphate dehydrogenase (glyceraldehyde-3-phosphate, NAD+, Pi) Triosephosphate isomerase (dihydroxyacetone phosphate) Phosphoglycerate kinase (1,3bisphospho glycerate, ADP) Phosphoglycerate mutase (3phosphoglycerate) Enolase (2-phosphoglycerate)TDH1 TDH2 TDH3 TPI PGK1 GPM1 ENO1 ENOYJL052W YJR009C YGR192C YDR050C YCR012W YKL152C YGR254W YHR174W7/11 (31.4) 8/11 (31.eight) 9/11 (35.9) 3/11 (31.eight) 6/11 (44.1) 4/11 (34.five) 5/11 (40) 5/11 (40) Glycolytic enzymes, pyrimidinerich (localization to G-bodies) A number of glycolytic proteins Fuller et al. 2020 (PARCLIP-seq) Matia-Gonz ez et al. 2015 (fluorescencebased protein NA interaction assay [RIP], RIP-qPCR) Entelis et al.tRK1 (import into mitochondria) Pyruvate kinase (phosphoenolpyruvate, ADP) PYK1 PYK2 YAL038W YOR347C 4/11 (33.6) 2/11 (20.9)relevance or point to methodological shortcomings or variations. A further open query concerns the specificity of binding, due to the fact certain RNA binding substrates are unknown for several glycolytic enzymes like for many metabolic enzymes. They may function either as specific RBPs targeting chosen RNAs or as nonspecific RBPs recognizing a broad spectrum of RNA species. These two distinctive modes of action may possibly come as well as distinct implications of moonlighting functions of glycolytic enzymes in RNA binding. On the one hand, RNA-binding enzymes could serve as scaffolds for macromolecular structure formation through numerous intermolecular interactions, thereby, regulating either RNA state or protein localization and metabolic activity. This situation mightmainly involve nonspecific RNA-binding processes if we take into consideration that the majority of the glycolytic enzymes are extremely abundant and as a result the molar ratio of enzyme to particular transcript is generally rather higher. Unspecific binding to various RNAs would raise the number of RNA substrates and facilitate effective regulation from the metabolic activity of your protein. Alternatively, binding to certain RNA could enable targeted regulation of RNA fate and activity.Neuromedin B manufacturer Due to the fact naked RNA inside the cell seems to be the rare exception as an alternative to the frequent form, a competitive method in between specific and common RNA-binding proteins has to be anticipated and could possibly be determinant in the occupation from the accessible RNA surfaces with glycolytic enzymes.Capreomycin Inhibitor rnajournal.PMID:23074147 orgWegener and DietzTABLE 3. Compilation of human glycolytic enzyme isoforms, their substrates, ID, presence in the RBP2GO (Caudron-Herger et al. 2020) database and info on reported functions Enzyme (substrate, cofactor) Hexokinase (glucose, ATP) HK1 HK2 HK3 GPI PFKL PFKM PFKP ALDOA ALDOB ALDOC GAPDH Isoform UniProt ID P19367 P52789 P52790 P06744 P17858 P08237 Q01813 P04075 P05062 P09972 P04406 RBP2GO (score) 4/43 (7.9) 5/43 (9) 0/43 (two.six) 6/43 (12.7) 3/43 (11.2) 2/43 (13.1) 6/43 (15.7) 13/43 (26.4) 0/43 (four.5) 7/43 (17.1) 16/43 (30.7) MyHC 3’UTR (localization to cytoskeleton) tRNA (nuclear export).