![]() ![]() Previous solution NMR and X-ray crystallography studies have shown that RRMs are globular domains, each composed of 4 anti-parallel β sheets that are backed by 2 α-helices. RRM is the most common motifs for RNA recognition and is usually made up of 90-100 amino acids. Structure RRM 1 and 2 connected by a short linker showing binding to the polyadenylate RNA.Ĭytosolic poly-A binding protein (PABPC) is made up of four RNA recognition motifs (RRMs) and a C-terminal region known as the PABC domain. Without these two proteins in-tandem, then the poly(A) tail would not be added and the RNA would degrade quickly. The poly(A)-binding protein may also protect the tail from degradation and regulate mRNA production. ![]() Poly(A)-binding protein is also present during stages of mRNA metabolism including nonsense-mediated decay and nucleocytoplasmic trafficking. The nuclear isoform selectively binds to around 50 nucleotides and stimulates the activity of polyadenylate polymerase by increasing its affinity towards RNA. The binding protein is also involved in mRNA precursors by helping polyadenylate polymerase add the poly(A) nucleotide tail to the pre-mRNA before translation. The poly(A) tail is located on the 3' end of mRNA and was discovered by Mary Edmonds, who also characterized the poly-A polymerase enzyme that generates the poly(a) tail. Poly(A)-binding protein ( PAB or PABP) is an RNA-binding protein which triggers the binding of eukaryotic initiation factor 4 complex (eIF4G) directly to the poly(A) tail of mRNA which is 200-250 nucleotides long. RNA binding protein Poly(A) RNA binding protein PABP (PDB 1CVJ) ![]()
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