https://scholars.lib.ntu.edu.tw/handle/123456789/638315
Title: | The Prp19-associated complex is required for specifying interactions of U5 and U6 with pre-mRNA during spliceosome activation | Authors: | SHIH-PENG CHAN Cheng, Soo-Chen |
Issue Date: | 2-Sep-2005 | Journal Volume: | 280 | Journal Issue: | 35 | Source: | The Journal of biological chemistry | Abstract: | Activation of the spliceosome involves a major structural change in the spliceosome, including release of U1 and U4 small nuclear ribonucleoprotein particles and the addition of a large protein complex, the Prp19-associated complex. We previously showed that the Prp19-associated complex is required for stable association of U5 and U6 with the spliceosome after U4 is released. Changes within the spliceosome upon binding of the Prp19-associated complex include remodeling of the U6/5' splice site interaction and destabilization of Lsm proteins to allow further interaction of U6 with the intron sequence. Here, we further analyzed interactions of U5 and U6 with pre-mRNA at various stages of spliceosome assembly from initial binding of tri-small nuclear ribonucleoprotein complex to the activated spliceosome to reveal stepwise changes of interactions. We demonstrate that both U5 and U6 interacted with pre-mRNA in dynamic manners spanning over a large region of U6 and the 5' exon sequences prior to the activation of the spliceosome. During spliceosome activation, interactions were locked down to small regions, and the Prp19-associated complex was required for defining the specificity of interaction of U5 and U6 with the 5' splice site to stabilize their association with the spliceosome after U4 is dissociated. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/638315 | ISSN: | 0021-9258 | DOI: | 10.1074/jbc.M505060200 |
Appears in Collections: | 微生物學科所 |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.