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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). 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.

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Tauchert, M. J., Author
Fourmann, J. B.1, Author           
Christian, H., Author
Lührmann, R.1, Author           
Ficner, R., Author
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1Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578576              

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Free keywords: Spliceosome; RNA helicase; DEAH-box protein; DHX15
 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.

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Language(s): eng - English
 Dates: 2016-02-222016-02
 Publication Status: Issued
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S2053230X15024498
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Title: Acta Crystallographica Section F
Source Genre: Journal
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Pages: - Volume / Issue: 72 (2) Sequence Number: - Start / End Page: 112 - 120 Identifier: -