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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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 Urheber:
Warkocki, Z.1, Autor           
Schneider, C.1, Autor           
Mozaffari-Jovin, S.1, Autor           
Schmitzova, J.1, Autor           
Höbartner, C.2, Autor           
Fabrizio, P.1, Autor           
Lührmann, R.1, Autor           
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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Schlagwörter: spliceosome activation, DEAH-box helicase, Prp2, G-patch protein, Spp2, ATP hydrolysis
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2015-01-012015-01
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1101/gad.253070.114
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Titel: Genes and Development
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 29 (1) Artikelnummer: - Start- / Endseite: 94 - 107 Identifikator: -