Molecular architecture and assembly of the human RNA Degradosome

Authors

Gee, J. A., Williams, J. G., Pillon, M. C.

Abstract

The PNPase exoribonuclease interacts with the SUV3 helicase to form the human RNA Degradosome responsible for processive mitochondrial RNA turnover and quality control. Although structural data reveals the trimeric PNPase architecture along with the monomeric and dimeric states of SUV3, the molecular basis of their assembly for processive RNA degradation remains poorly understood. Here we present the molecular characterization of the human RNA Degradosome and define critical molecular features that regulate complex formation. We identify the protein regions required for RNA Degradosome formation and establish the minimum components necessary for the SUV3-PNPase interaction. Chemical crosslinking mass spectrometry analysis reveals distance restraints that position the SUV3 N-terminal domain alongside of the PNPase S1 domain, defining an important interface for complex formation. These findings provide mechanistic insight into how PNPase and SUV3 assemble to form the human RNA Degradosome.

Preprint server: bioRxiv
The authors list and abstract were imported from bioRxiv on 07 Sep 2026.

Stats

1-terrible, 9-excellent. How would you rate this preprint? Sign in in to submit your rating.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.