8RDY

Saccharomyces cerevisiae Prp43 helicase in complex with Pxr1

Summary for 8RDY

• Entry DOI: 10.2210/pdb8rdy/pdb
• EMDB information: 19078
• Descriptor: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43, Glutathione S-transferase class-mu 26 kDa isozyme,Protein PXR1, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: preribosome, helicase, ribosome assembly, inhibitor, rna binding protein
• Biological source: Saccharomyces cerevisiae (brewer's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 134445.36

Authors

Rabl, J.,Portugal Calisto, D.,Panse, V.G. (deposition date: 2023-12-08, release date: 2024-10-23, Last modification date: 2024-12-04)

Primary citation

Portugal-Calisto, D.,Geiger, A.G.,Rabl, J.,Vadas, O.,Oborska-Oplova, M.,Mazur, J.,Richina, F.,Klingauf-Nerurkar, P.,Michel, E.,Leitner, A.,Boehringer, D.,Panse, V.G.
An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly.
Nat Commun, 15:10150-10150, 2024

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, 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.

PubMed: 39578461
DOI: 10.1038/s41467-024-54584-5

Experimental method

ELECTRON MICROSCOPY (3.33 Å)