Journal article

Publication year: 2004

Pages: 7392-7401

Journal: Molecular and Cellular Biology

Volume number: 24

Issue number: 17

ISSN: 0270-7306

eISSN: 1098-5549

Open access status: Green

DOI Link: https://doi.org/10.1128/MCB.24.17.7392-7401.2004

Publisher: Taylor and Francis Group

Abstract: 
After each spliceosome cycle, the U4 and U6 snRNAs are released separately and are recycled to the functional U4/U6 snRNP, requiring in the mammalian system the U6-specific RNA binding protein p110 (SART3). Its domain structure is made up of an extensive N-terminal domain with at least seven tetratricopeptide repeat (TPR) motifs, followed by two RNA recognition motifs (RRMs) and a highly conserved C-terminal sequence of 10 amino acids. Here we demonstrate under in vitro recycling conditions that U6-p110 is an essential splicing factor. Recycling activity requires both the RRMs and the TPR domain but not the highly conserved C-terminal sequence. For U6-specific RNA binding, the two RRMs with some flanking regions are sufficient. Yeast two-hybrid assays reveal that p110 interacts through its TPR domain with the U4/U6-specific 90K protein, indicating a specific role of the TPR domain in spliceosome recycling. On the 90K protein, a short internal region (amino acids 416 to 550) suffices for the interaction with p110. Together, these data suggest a model whereby p110 brings together U4 and U6 snRNAs through both RNA-protein and protein-protein interactions.

Harvard Citation style: Medenbach, J., Schreiner, S., Liu, S., Lührmann, R. and Bindereif, A. (2004) Human U4/U6 snRNP recycling factor p110: Mutational analysis reveals the function of the tetratricopeptide repeat domain in recycling, Molecular and Cellular Biology, 24(17), pp. 7392-7401. https://doi.org/10.1128/MCB.24.17.7392-7401.2004

APA Citation style: Medenbach, J., Schreiner, S., Liu, S., Lührmann, R., & Bindereif, A. (2004). Human U4/U6 snRNP recycling factor p110: Mutational analysis reveals the function of the tetratricopeptide repeat domain in recycling. Molecular and Cellular Biology. 24(17), 7392-7401. https://doi.org/10.1128/MCB.24.17.7392-7401.2004