TAILIEUCHUNG - Báo cáo y học: "Identification of motifs that function in the splicing of non-canonical introns"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Minireview cung cấp cho các bạn kiến thức về ngành y đề tài: Identification of motifs that function in the splicing of non-canonical introns. | Open Access Identification of motifs that function in the splicing of non-canonical introns Jill I Murray Rodger B Voelker Kristy L Henscheid M Bryan Warf and J Andrew Berglund Address Institute of Molecular Biology and Department of Chemistry University of Oregon Eugene Oregon USA. Correspondence J Andrew Berglund. Email aberglund@ Published 12 June 2008 Genome Biology 2008 9 R97 doi 186 gb-2008-9-6-r97 The electronic version of this article is the complete one and can be found online at http 2008 9 6 R97 Received 20 September 2007 Revised 27 December 2007 Accepted 12 June 2008 2008 Murray et al. licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background While the current model of pre-mRNA splicing is based on the recognition of four canonical intronic motifs 5 splice site branchpoint sequence polypyrimidine PY tract and 3 splice site it is becoming increasingly clear that splicing is regulated by both canonical and non-canonical splicing signals located in the RNA sequence of introns and exons that act to recruit the spliceosome and associated splicing factors. The diversity of human intronic sequences suggests the existence of novel recognition pathways for non-canonical introns. This study addresses the recognition and splicing of human introns that lack a canonical PY tract. The PY tract is a uridine-rich region at the 3 end of introns that acts as a binding site for U2AF65 a key factor in splicing machinery recruitment. Results Human introns were classified computationally into low- and high-scoring PY tracts by scoring the likely U2AF65 binding site strength. Biochemical studies confirmed that low-scoring PY tracts are weak U2AF65 binding sites while high-scoring PY .

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