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Structural analysis of the intrinsically disordered splicing factor Spp2 and its complex with the DEAH-box ATPase Prp2

ABSTRACT: Structural analysis of spp2 bound to prp2 with chemical crosslinking and mass spectrometry

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Chaetomium Thermophilum (strain Dsm 1495 / Cbs 144.50 / Imi 039719)

SUBMITTER: Romina Hofele

LAB HEAD: Prof. Dr. Henning Urlaub

PROVIDER: PXD015793 | Pride | 2020-05-27

REPOSITORIES: Pride

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	RHofele_ctprp2_spp2_021112_BS3.mgf	Mgf
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	RHofele_ctprp2_spp2_021112_BS3.raw	Raw
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Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2.

Hamann Florian F Schmitt Andreas A Favretto Filippo F Hofele Romina R Neumann Piotr P Xiang ShengQi S Urlaub Henning H Zweckstetter Markus M Ficner Ralf R

Proceedings of the National Academy of Sciences of the United States of America 20200123 6

The spliceosome consists of five small RNAs and more than 100 proteins. Almost 50% of the human spliceosomal proteins were predicted to be intrinsically disordered or to contain disordered regions, among them the G-patch protein Spp2. The G-patch region of Spp2 binds to the DEAH-box ATPase Prp2, and both proteins together are essential for promoting the transition from the B<sup>act</sup> to the catalytically active B* spliceosome. Here we show by circular dichroism and nuclear magnetic resonanc ...[more]

PMID: 31974312

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