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Journal Article

Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum.

MPS-Authors
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Fourmann,  J. B.
Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Lührmann,  R.
Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

2253003.pdf
(Publisher version), 3MB

Supplementary Material (public)

2253003_Suppl.pdf
(Supplementary material), 444KB

Citation

Tauchert, M. J., Fourmann, J. B., Christian, H., Lührmann, R., & Ficner, R. (2016). Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum. Acta Crystallographica Section F, 72(2), 112-120. doi:10.1107/S2053230X15024498.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-C6DE-2
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.