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- W2118317659 abstract "The human hnRNP C is a ubiquitous cellular protein involved in mRNA maturation. Recently, we have shown that this protein specifically recognizes uridine (U) pentamers through its single RNA recognition motif (RRM). However, a large fraction of natural RNA targets of hnRNP C consists of much longer contiguous uridine stretches. To understand how these extended sites are recognized, we studied the binding of the RRM to U-tracts of 8-11 bases. In vivo investigation of internal translation activation of unr (upstream of N-ras) mRNA indicates that the conservation of the entire hnRNP C binding site, UC(U)8, is required for hnRNP C-dependent IRES activation. The assays further suggest a synergistic interplay between hnRNP C monomers, dependent on the protein's ability to oligomerize. In vitro spectroscopic and thermodynamic analyses show that isolated RRMs bind to (U)11 oligomers as dimers. Structural modeling of a ternary double-RRM/RNA complex indicates additionally that two RRM copies can be accommodated on the canonical sequence UC(U)8. The proposed tandem RRM binding is in very good agreement with the transcriptome-wide recognition of extended U-tracts by full-length hnRNP C, which displays a cross-linking pattern consistent with a positively cooperative RRM dimer binding model." @default.
- W2118317659 created "2016-06-24" @default.
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- W2118317659 date "2015-09-14" @default.
- W2118317659 modified "2023-10-17" @default.
- W2118317659 title "Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing" @default.
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- W2118317659 doi "https://doi.org/10.1261/rna.052373.115" @default.
- W2118317659 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4604433" @default.
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