TAILIEUCHUNG - Báo cáo khoa học: A structured RNA in hepatitis B virus post-transcriptional regulatory element represses alternative splicing in a sequence-independent and position-dependent manner

Hepatitis B virus (HBV) transcripts are subjected to multiple splicing deci-sions, but the mechanism of splicing regulation remains poorly understood. In this study, we used a well-investigated alternative splicing reporter to dissect splicing regulatory elements residing in the post-transcriptional reg-ulatory element (PRE) of HBV. | BFEBS Journal A structured RNA in hepatitis B virus post-transcriptional regulatory element represses alternative splicing in a sequence-independent and position-dependent manner Chen Huang1 2 Mao-Hua Xie1 Wei Liu1 Bo Yang1 Fan Yang1 Jingang Huang1 Jie Huang1 Qijia Wu1 Xiang-Dong Fu1 3 and Yi Zhang1 2 1 State Key Laboratory of Virology College of Life Sciences Wuhan University Hubei China 2 Center for Genome Analysis ABLife Inc. Dong-Hu-Ming-Ju Wuhan Hubei China 3 Department of Cellular and Molecular Medicine University of California San Diego La Jolla CA USA Keywords alternative splicing HBV PRE hepatitis B virus HBV intronic splicing silencer ISS RNA structure Correspondence Y. Zhang Center for Genome Analysis ABLife Inc. Dong-Hu-Ming-Ju Room 1-2-1202 18 North Zhuo-Dao-Quan Road Wuhan Hubei 430079 China Fax 86 27 68754945 Tel 86 27 87153085 E-mail yizhang101@ Received 1 October 2010 revised 3 November 2010 accepted 24 February 2010 doi Hepatitis B virus HBV transcripts are subjected to multiple splicing decisions but the mechanism of splicing regulation remains poorly understood. In this study we used a well-investigated alternative splicing reporter to dissect splicing regulatory elements residing in the post-transcriptional regulatory element PRE of HBV. A strong intronic splicing silencer ISS with a minimal functional element of 105 nucleotides referred to as PRE-ISS was identified and interestingly both the sense and antisense strands of the element were found to strongly suppress alternative splicing in multiple human cell lines. PRE-ISS folds into a double-hairpin structure in which substitution mutations disrupting the double-hairpin structure abolish the splicing silencer activity. Although it harbors two previously identified binding sites for polypyrimidine tract binding protein PRE-ISS represses splicing independent of this protein. The silencing function of PRE-ISS exhibited a strong position dependence .

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