

The C proteins of HeLa 40S nuclear ribonucleoprotein particles exist as anisotropic tetramers of (C1)3 C2. Solution structure of the symmetric coiled coil tetramer formed by the oligomerization domain of hnRNP C: implications for biological function. Examining physical parameters of protein–nucleic acid complexes. Laser cross-linking of proteins to nucleic acids. Hockensmith, J.W., Kubasek, W.L., Vorachek, W.R. Methodology and first applications to the phage T4 DNA replication system. Laser cross-linking of nucleic acids to proteins. Mutational definition of RNA-binding and protein–protein interaction domains of heterogeneous nuclear RNP C1. The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins. Interaction of the RNA-binding domain of the hnRNP C proteins with RNA. Gorlach, M., Wittekind, M., Beckman, R.A., Mueller, L. Nucleolin and heterogeneous nuclear ribonucleoprotein C proteins specifically interact with the 3′-untranslated region of amyloid protein precursor mRNA. Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner. Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping. A two-tracked approach to analyze RNA-protein crosslinking sites in native, nonlabeled small nuclear ribonucleoprotein particles.
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An RNA code for the FOX2 splicing regulator revealed by mapping RNA-protein interactions in stem cells. HITS-CLIP yields genome-wide insights into brain alternative RNA processing. CLIP: A method for identifying protein–RNA interaction sites in living cells. CLIP identifies Nova-regulated RNA networks in the brain. Independent deposition of heterogeneous nuclear ribonucleoproteins and small nuclear ribonucleoprotein particles at sites of transcription. Mechanisms of fidelity in pre-mRNA splicing. The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles. Arrangement of 30S heterogeneous nuclear ribonucleoprotein on polyoma virus late nuclear transcripts. Identification and characterization of the packaging proteins of core 40S hnRNP particles. Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches. The spliceosome: design principles of a dynamic RNP machine. Expansion of the eukaryotic proteome by alternative splicing.

The ability of high-resolution iCLIP data to provide insights into the mechanism of this regulation holds promise for studies of other higher-order ribonucleoprotein complexes. Integration of transcriptome-wide iCLIP data and alternative splicing profiles into an 'RNA map' indicates how the positioning of hnRNP particles determines their effect on the inclusion of alternative exons. hnRNP particles assemble on both introns and exons but remain generally excluded from splice sites. iCLIP data show that hnRNP C recognizes uridine tracts with a defined long-range spacing consistent with hnRNP particle organization. Here, we developed individual-nucleotide resolution UV cross-linking and immunoprecipitation (iCLIP) to study the role of hnRNP C in splicing regulation. Despite their abundance, however, it remained unclear whether these particles control pre-mRNA processing. In the nucleus of eukaryotic cells, nascent transcripts are associated with heterogeneous nuclear ribonucleoprotein (hnRNP) particles that are nucleated by hnRNP C.
