An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly

Daniela Portugal-Calisto, Alexander Gregor Geiger, Julius Rabl, Oscar Vadas, Michaela Oborská-Oplová, Jarosław Mazur, Federica Richina, Purnima Klingauf-Nerurkar, Erich Michel, Alexander Leitner, Daniel Boehringer and Vikram Govind Panse ()
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Daniela Portugal-Calisto: University of Zurich
Alexander Gregor Geiger: University of Zurich
Julius Rabl: ETH Zurich
Oscar Vadas: University of Geneva
Michaela Oborská-Oplová: University of Zurich
Jarosław Mazur: University of Zurich
Federica Richina: ETH Zurich
Purnima Klingauf-Nerurkar: University of Zurich
Erich Michel: University of Zurich
Alexander Leitner: ETH Zurich
Daniel Boehringer: ETH Zurich
Vikram Govind Panse: University of Zurich

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract Mechanisms by which G-patch activators tune the processive multi-tasking ATP-dependent RNA helicase Prp43 (DHX15 in humans) to productively remodel diverse RNA:protein complexes remain elusive. Here, a comparative study between a herein and previously characterized activators, Tma23 and Pxr1, respectively, defines segments that organize Prp43 function during ribosome assembly. In addition to the activating G-patch, we discover an inhibitory segment within Tma23 and Pxr1, I-patch, that restrains Prp43 ATPase activity. Cryo-electron microscopy and hydrogen-deuterium exchange mass spectrometry show how I-patch binds to the catalytic RecA-like domains to allosterically inhibit Prp43 ATPase activity. Tma23 and Pxr1 contain dimerization segments that organize Prp43 into higher-order complexes. We posit that Prp43 function at discrete locations on pre-ribosomal RNA is coordinated through toggling interactions with G-patch and I-patch segments. This could guarantee measured and timely Prp43 activation, enabling precise control over multiple RNA remodelling events occurring concurrently during ribosome formation.

Date: 2024
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DOI: 10.1038/s41467-024-54584-5

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