tailieunhanh - Báo cáo y học: "Alternative splicing of mouse transcription factors affects their DNA-binding domain architecture and is tissue specific"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Alternative splicing of mouse transcription factors affects their DNA-binding domain architecture and is tissue specific. | Research Open Access Alternative splicing of mouse transcription factors affects their DNA-binding domain architecture and is tissue specific Bahar Taneri Ben Snyder Alexey Novoradovsky and Terry Gaasterland Addresses The Laboratory of Computational Genomics The Rockefeller University New York NY 10021 USA. tScripps Institution of Oceanography University of California San Diego La Jolla CA 92093 USA. Correspondence Terry Gaasterland. E-mail gaasterl@ Received 28 May 2004 Revised 1 7 August 2004 Accepted 18 August 2004 Published 30 September 2004 Genome Biology 2004 5 R75 The electronic version of this article is the complete one and can be found online at http 2004 5 10 R75 2004 Taneri 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. I III I II Hill Abstract Background Analyzing proteins in the context of all available genome and transcript sequence data has the potential to reveal functional properties not accessible through protein sequence analysis alone. To analyze the impact of alternative splicing on transcription factor TF protein structure we constructed a comprehensive database of splice variants in the mouse transcriptome called MouSDB3 containing 461 TF loci. Results Our analysis revealed that 62 of these loci in MouSDB3 have variant exons compared to 29 of all loci. These variant TF loci contain a total of 324 alternative exons of which 23 are in-frame. When excluded 80 of in-frame alternative exons alter the domain architecture of the protein as computed by SMART simple modular architecture research tool . Sixty-eight of these exons directly affect the coding regions of domains important for TF function. Seventy-five of the domains affected are DNA-binding domains.