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biorxiv2026-09-06mtRNARNA decaystructural biology

SUV3 N-terminus docks PNPase S1 domain to build the human mitochondrial RNA degradosome

Processive mitochondrial RNA turnover is a PNPase-SUV3 machine. This paper names the minimum parts and, with crosslinking mass spectrometry, parks the SUV3 N-terminal domain against the PNPase S1 domain.

Mito.news · at a glance

Signal profile (abstract-level)

mtRNA · RNA decay · structural biology

Score 81/100BIORXIVhigh confidencemtRNA
81
Importance
50
Mito signal
39
Dysfunction
64
Evidence
30
Translational

Editorial signal profile from the abstract (importance score, mito keywords, dysfunction tags, evidence density, translational cues). Not a figure reproduced from the preprint PDF.

Finding. Mitochondrial RNA is chewed by a degradosome of PNPase and SUV3. Gee, Williams and Pillon map how those two hold each other. They name the regions you need, the smallest set that still binds, and, with crosslinking mass spectrometry, put the SUV3 N-terminal domain beside the PNPase S1 domain.

Score 81. Core mtRNA machine, a contact, XL-MS. High confidence for the interface as stated.

What to do with it Build the minimum complex. Mutate the S1-NTD pair. Dock PNPT1/SUV3 missense variants on that surface.

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Source preprint

Molecular architecture and assembly of the human RNA Degradosome

10.64898/2026.09.03.749114

Gee JA, Williams JG, Pillon MC.

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