Identification of a novel component C2ORF3 in the lariat–intron complex: lack of C2ORF3 interferes with pre‐mRNA splicing via intron turnover pathway |
| |
| Authors: | Rei Yoshimoto Katsuya Okawa Minoru Yoshida Mutsuhito Ohno Naoyuki Kataoka |
| |
| Institution: | 1. Chemical Genetics Laboratory, RIKEN Advanced Science Institute, , Wako, Saitama, 351‐0198 Japan;2. Institute for Virus Research, Kyoto University, , Sakyo‐ku, Kyoto, 606‐8507 Japan;3. Drug Research Laboratories, Kyowa Hakko Kirin Co., Ltd, , Nagaizumi, Shizuoka, 411‐8731 Japan;4. Laboratory for Malignancy Control Research, Medical Innovation Center, Kyoto University Graduate School of Medicine, , Sakyo‐ku, Kyoto, 606‐8507 Japan |
| |
| Abstract: | To identify the novel factors involved in the postsplicing intron turnover pathway, we carried out immunoprecipitation with known postsplicing factors, hPrp43 and TFIP11. As an interacting factor, we identified C2ORF3 protein by mass spectrometry. We found that C2ORF3 protein is present in the previously characterized Intron Large (IL) complex with an excised lariat intron. In vitro splicing using C2ORF3‐depleted nuclear extracts showed significant repression of splicing, suggesting that C2ORF3 protein is required for pre‐mRNA splicing through its presumable role in efficient intron turnover. Interestingly, C2ORF3 protein is localized in both the nucleoplasm and nucleoli, which suggests a potential function in rRNA processing. |
| |
| Keywords: | |
|
|
