Abstract 1680 Analysis of deletion of the Lsm7 protein from the Lsm2-8 heteroheptamer
Lsm2-8 is a protein complex essential in the spliceosome and pre-mRNA processing, forming a key component of the U6 snRNP alongside Prp24. Lsm2-8 binds to the 3' end of U6 snRNA and increases the rate of U4/U6 annealing when working in collaboration with Prp24. This study investigates the structural and functional consequences of deleting Lsm7, a component of the Lsm2-8 complex, in Saccharomyces cerevisiae. Through the purification of Lsm2-8 complexes lacking Lsm7 (Δ7), we identified subpopulations of complexes with varying structural configurations.
Authors
- Yuichiro Nomura (ORCID: https://orcid.org/0000-0002-8275-4468)
- Aaron A. Hoskins (ORCID: https://orcid.org/0000-0002-9777-519X)
- Yujing Liu (ORCID: https://orcid.org/0000-0002-4845-6643)
- Samuel Butcher (ORCID: https://orcid.org/0000-0002-3373-6220)
- Marisse Covin
Institutions
- University of Wisconsin System (US)
- University of Wisconsin–Madison (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109915
- Primary Topic
- Glycosylation and Glycoproteins Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00