tailieunhanh - Báo cáo y học: "The SR protein family"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Wertheim cung cấp cho các bạn kiến thức về ngành y đề tài: The SR protein family. | X Genome Biology Protein family review The SR protein family Peter J Shepard and Klemens J Hertel Address Department of Microbiology and Molecular Genetics University of California Irvine Irvine CA 92697-4025 USA. Correspondence Klemens J Hertel. Email khertel@ Summary The processing of pre-mRNAs is a fundamental step required for the expression of most metazoan genes. Members of the family of serine arginine SR -rich proteins are critical components of the machineries carrying out these essential processing events highlighting their importance in maintaining efficient gene expression. SR proteins are characterized by their ability to interact simultaneously with RNA and other protein components via an RNA recognition motif RRM and through a domain rich in arginine and serine residues the RS domain. Their functional roles in gene expression are surprisingly diverse ranging from their classical involvement in constitutive and alternative pre-mRNA splicing to various post-splicing activities including mRNA nuclear export nonsense-mediated decay and mRNA translation. These activities point up the importance of SR proteins during the regulation of mRNA metabolism. Gene organization and evolutionary history The discovery of SR proteins goes back to studies in Drosophila where genetic screens identified SWAP suppressor-of-white-apricot 1 Tra transformer 2 and Tra-2 transformer-2 3 as splicing factors. Their sequence characterization led to the identification of a protein domain rich in arginine and serine dipeptides termed the arginine serine RS domain. Subsequent identification of the splicing factors SF2 ASF and SC35 from human cell lines also revealed the presence of extended RS domains in addition to at least one RNA-binding domain of the RNA recognition motif RRM -type 4-6 . The family of SR proteins was classified following the identification of additional RS-domain-containing proteins on the basis of the presence of a phosphoepitope recognized by the .

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