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Acta Crystallogr F Struct Biol Commun. 2016 Feb;72(Pt 2):112-20. doi: 10.1107/S2053230X15024498. Epub 2016 Jan 22.

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

Author information

1
Department of Molecular Structural Biology, Institute for Microbiology and Genetics, GZMB, Georg-August-Universität Göttingen, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany.
2
Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

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 Å 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.

KEYWORDS:

DEAH-box protein; DHX15; RNA helicase; spliceosome

PMID:
26841761
PMCID:
PMC4741191
DOI:
10.1107/S2053230X15024498
[Indexed for MEDLINE]
Free PMC Article

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