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.
| Original language | English |
|---|---|
| Pages (from-to) | 78-87 |
| Number of pages | 10 |
| Journal | Genes to Cells |
| Volume | 19 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 01-01-2014 |
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All Science Journal Classification (ASJC) codes
- Genetics
- Cell Biology
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Identification of a novel component C2ORF3 in the lariat-intron complex : Lack of C2ORF3 interferes with pre-mRNA splicing via intron turnover pathway. / Yoshimoto, Rei; Okawa, Katsuya; Yoshida, Minoru; Ohno, Mutsuhito; Kataoka, Naoyuki.
In: Genes to Cells, Vol. 19, No. 1, 01.01.2014, p. 78-87.Research output: Contribution to journal › Article
TY - JOUR
T1 - Identification of a novel component C2ORF3 in the lariat-intron complex
T2 - Lack of C2ORF3 interferes with pre-mRNA splicing via intron turnover pathway
AU - Yoshimoto, Rei
AU - Okawa, Katsuya
AU - Yoshida, Minoru
AU - Ohno, Mutsuhito
AU - Kataoka, Naoyuki
PY - 2014/1/1
Y1 - 2014/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=84891150041&partnerID=8YFLogxK
U2 - 10.1111/gtc.12114
DO - 10.1111/gtc.12114
M3 - Article
C2 - 24304693
AN - SCOPUS:84891150041
VL - 19
SP - 78
EP - 87
JO - Genes to Cells
JF - Genes to Cells
SN - 1356-9597
IS - 1
ER -