Premium
Identification of a novel component C2ORF3 in the lariat–intron complex: lack of C2ORF3 interferes with pre‐m RNA splicing via intron turnover pathway
Author(s) -
Yoshimoto Rei,
Okawa Katsuya,
Yoshida Minoru,
Ohno Mutsuhito,
Kataoka Naoyuki
Publication year - 2014
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12114
Subject(s) - intron , rna splicing , biology , nucleoplasm , nucleolus , splicing factor , microbiology and biotechnology , precursor mrna , protein splicing , immunoprecipitation , messenger rna , gene , genetics , rna , nucleus
To identify the novel factors involved in the postsplicing intron turnover pathway, we carried out immunoprecipitation with known postsplicing factors, hP rp43 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.