Literature DB >> 26841761

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

Marcel J Tauchert1, Jean-Baptiste Fourmann2, Henning Christian1, Reinhard Lührmann2, Ralf Ficner1.   

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.

Entities:  

Keywords:  DEAH-box protein; DHX15; RNA helicase; spliceosome

Mesh：

Substances：

Year:  2016        PMID： 26841761      PMCID： PMC4741191          DOI： 10.1107/S2053230X15024498

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN： 2053-230X            Impact factor:   1.056


  41 in total

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  14 in total

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3.  The G-patch activators Pfa1 and PINX1 exhibit different modes of interaction with the Prp43 RNA helicase.

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5.  Structural insights into the mechanism of the DEAH-box RNA helicase Prp43.

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6.  Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.

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7.  Regulation of Prp43-mediated disassembly of spliceosomes by its cofactors Ntr1 and Ntr2.

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8.  Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.

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9.  Structural basis of G-quadruplex unfolding by the DEAH/RHA helicase DHX36.

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10.  Crystal structure of the spliceosomal DEAH-box ATPase Prp2.

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