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  The G-patch protein Spp2 couples the spliceosome-stimulated ATPase activity of the DEAH-box protein Prp2 to catalytic activation of the spliceosome.

Warkocki, Z., Schneider, C., Mozaffari-Jovin, S., Schmitzova, J., Höbartner, C., Fabrizio, P., et al. (2015). The G-patch protein Spp2 couples the spliceosome-stimulated ATPase activity of the DEAH-box protein Prp2 to catalytic activation of the spliceosome. Genes and Development, 29(1), 94-107. doi:10.1101/gad.253070.114.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-6859-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-27EB-4
Genre: Journal Article

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Warkocki, Z.1, Author              
Schneider, C.1, Author              
Mozaffari-Jovin, S.1, Author              
Schmitzova, J.1, Author              
Höbartner, C.2, Author              
Fabrizio, P.1, Author              
Lührmann, R.1, Author              
Affiliations:
1Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
2Research Group of Nucleic Acid Chemistry, MPI for biophysical chemistry, Max Planck Society, ou_578605              

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Free keywords: spliceosome activation, DEAH-box helicase, Prp2, G-patch protein, Spp2, ATP hydrolysis
 Abstract: Structural rearrangement of the activated spliceosome (B(act)) to yield a catalytically active complex (B*) is mediated by the DEAH-box NTPase Prp2 in cooperation with the G-patch protein Spp2. However, how the energy of ATP hydrolysis by Prp2 is coupled to mechanical work and what role Spp2 plays in this process are unclear. Using a purified splicing system, we demonstrate that Spp2 is not required to recruit Prp2 to its bona fide binding site in the B(act) spliceosome. In the absence of Spp2, the B(act) spliceosome efficiently triggers Prp2's NTPase activity, but NTP hydrolysis is not coupled to ribonucleoprotein (RNP) rearrangements leading to catalytic activation of the spliceosome. Transformation of the B(act) to the B* spliceosome occurs only when Spp2 is present and is accompanied by dissociation of Prp2 and a reduction in its NTPase activity. In the absence of spliceosomes, Spp2 enhances Prp2's RNA-dependent ATPase activity without affecting its RNA affinity. Our data suggest that Spp2 plays a major role in coupling Prp2's ATPase activity to remodeling of the spliceosome into a catalytically active machine.

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Language(s): eng - English
 Dates: 2015-01-012015-01
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1101/gad.253070.114
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Title: Genes and Development
Source Genre: Journal
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Pages: - Volume / Issue: 29 (1) Sequence Number: - Start / End Page: 94 - 107 Identifier: -