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This galley proof is being listed electronically before publishing the final manuscript (It's not final version).

Relative strength of 5’ splice-site strength defines functions of SRSF2 and SRSF6 in alternative splicing of Bcl-x pre-mRNA
haihong Shen 7,7,* (gwangju institute of science and technology), namjeong choi1,1,1 (gwangju institute of science and technology), yongchao liu2,2,2 (gwangju institute of science and technology), jagyeong oh3,3,3 (gwangju institute of science and technology), jiyeon ha4,4,4 (gwangju institute of science and technology), claudia ghigna5,5,5 (Institute of Molecular Genetics , national research council, italy), xuexiu zheng6,6,6 (gwangju institute of science and technology)
1life sciences, gwangju institute of science and technology
Bcl-x, a member of the Bcl-2 family, plays a key role in apoptosis. Alternative splicing of Bcl-x pre-mRNA through alternative 5’ splice-site selection produces an anti-apoptotic mRNA isoform that includes exon 2b and a pro-apoptotic Bcl-x mRNA isoform that excludes exon 2b. Here we used Bcl-x minigene and identified SRSF2 and SRSF6 as two regulatory factors of 5’ splice-site selection of Bcl-x pre-mRNA. We selected binding clusters closer to 5’ splice-sites from multiple potential binding sites of SRSF2 and SRSF6 to perform loss of functions analysis through site-directed mutagenesis. Our results demonstrated that these mutations did not abolish regulatory functions of SRSF2 or SRSF6, indicating that a single binding motif or a cluster was not a functional target of these proteins in Bcl-x pre-mRNA splicing. Random deletion mutagenesis did not disrupt the role of SRSF2 and SRSF6. Importantly, mutagenesis of 5’ splice-site to a conserved or a weaker score demonstrated that the weaker strength of the target 5’ splice-site or higher strength of the other 5’ splice-site strength limited the role of SRSF2 and SRSF6 in 5’ splice-site activation.
Abstract, Accepted Manuscript(in press) [Submitted on August 14, 2020, Accepted on October 12, 2020]
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