Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum
2016 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum
Tauchert, M. J. ; Fourmann, J.-B.; Christian, H.; Lührmann, R. & Ficner, R. (2016)
Acta Crystallographica Section F Structural Biology Communications, 72(2) pp. 112-120. DOI: https://doi.org/10.1107/S2053230X15024498
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Details
- Authors
- Tauchert, Marcel J. ; Fourmann, Jean-Baptiste; Christian, Henning; Lührmann, Reinhard ; Ficner, Ralf
- Abstract
- RNA helicases are indispensable for all organisms in each domain of life and have implications in numerous cellular processes. The DEAH-box RNA helicase Prp43 is involved in pre-mRNA splicing as well as rRNA maturation. Here, the crystal structure of Chaetomium thermophilum Prp43 at 2.9 angstrom resolution is revealed. Furthermore, it is demonstrated that Prp43 from C. thermophilum is capable of functionally replacing its orthologue from Saccharomyces cerevisiae in spliceosomal disassembly assays.
- Issue Date
- 2016
- Publisher
- Int Union Crystallography
- Journal
- Acta Crystallographica Section F Structural Biology Communications
- eISSN
- 2053-230X
- ISSN
- 2053-230X
