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RNA recognition motif, RNP-1 is a putative RNA-binding domain of about 90 amino acids that are known to bind single-stranded RNAs. It was found in many eukaryotic proteins. [ 1 ] [ 2 ] [ 3 ]
"Easy RNA Profile IdentificatioN" is an RNA motif search program reads a sequence alignment and secondary structure, and automatically infers a statistical "secondary structure profile" (SSP). An original Dynamic Programming algorithm then matches this SSP onto any target database, finding solutions and their associated scores.
Residues are numbered in increments of ten. The 5′- and 3′-ends are indicated. Highlighted are the two hinges and the small (Alu) and large (S, "specific") domain of the SRP RNA. The signal recognition particle RNA, (also known as 7SL, 6S, ffs, or 4.5S RNA) is part of the signal recognition particle (SRP) ribonucleoprotein complex.
The signal recognition particle (SRP) is an abundant, cytosolic, universally conserved ribonucleoprotein (protein-RNA complex) that recognizes and targets specific proteins to the endoplasmic reticulum in eukaryotes and the plasma membrane in prokaryotes.
Neuron-specific CELF family RNA-binding protein UNC-75 specifically binds to the UUGUUGUGUUGU mRNA stretch via its three RNA recognition motifs for the exon 7a selection in C. elegans' neuronal cells. As exon 7a is skipped due to its weak splice sites in non-neuronal cells, UNC-75 was found to specifically activate splicing between exon 7a and ...
Center for non-coding RNA in Technology and Health, University of Copenhagen: Yes Yes Yes All Yes NGG, NGA, NAG Yes Yes , [3] [4] Invitrogen TrueDesign Genome Editor Thermo Fisher Scientific: Yes Yes No 3 No NGG Yes Yes [5] Breaking-Cas Spanish National Center for Biotechnology: Yes (over 1000 genomes) Yes Yes (by weights) 4 No User ...
Termination of the polymerase. A number of factors which have been found to control how and when termination occurs, which will dictate the fate of the RNA transcript. All three of these systems work in concert to integrate signals from the cell and change the transcriptional program accordingly.
Cross-linking and immunoprecipitation (CLIP, or CLIP-seq) is a method used in molecular biology that combines UV crosslinking with immunoprecipitation in order to identify RNA binding sites of proteins on a transcriptome-wide scale, thereby increasing our understanding of post-transcriptional regulatory networks.