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Title | An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly. |
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Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 10150, Year 2024 |
Publish date | Nov 22, 2024 |
Authors | 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 / Vikram Govind Panse / |
PubMed 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, ...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. |
External links | Nat Commun / PubMed:39578461 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.33 Å |
Structure data | EMDB-19078, PDB-8rdy: |
Chemicals | ChemComp-ADP: ChemComp-MG: |
Source |
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Keywords | RNA BINDING PROTEIN / preribosome / helicase / ribosome assembly / inhibitor |