Structural highlights
Publication Abstract from PubMed
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 A 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.
Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum.,Tauchert MJ, Fourmann JB, Christian H, Luhrmann R, Ficner R Acta Crystallogr F Struct Biol Commun. 2016 Feb;72(Pt 2):112-20. doi:, 10.1107/S2053230X15024498. Epub 2016 Jan 22. PMID:26841761[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tauchert MJ, Fourmann JB, Christian H, Luhrmann R, Ficner R. Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum. Acta Crystallogr F Struct Biol Commun. 2016 Feb;72(Pt 2):112-20. doi:, 10.1107/S2053230X15024498. Epub 2016 Jan 22. PMID:26841761 doi:http://dx.doi.org/10.1107/S2053230X15024498
