ArticlePLoS pathogens2025
A non-classical PUF family protein in oomycetes functions as a pre-rRNA processing regulator and a target for RNAi-based disease control.
Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Ribosome biogenesis is an essential and tightly regulated process linked to cell proliferation and growth. However, its regulatory mechanisms in oomycetes, a group of organisms with significant agricultural and ecological importance, remain unclear. In this study, we identify Puf4, a non-classical PUF (Pumilio and FBF) family RNA-binding protein that plays a conserved and crucial role in pre-rRNA processing in oomycetes. Knockout of PuPuf4 in Pythium ultimum or its ortholog PsPuf4 in Phytophthora sojae results in defective vegetative growth, impaired development, and reduced pathogenicity. Specifically, PuPuf4 binds to the H68 component of 25S rRNA, and its knockout leads to overaccumulation of rRNA processing intermediates, including 5'ETS, ITS1, and ITS2 precursors. Additionally, the AG-rich motif identified as the first binding motif of L-shaped PUF proteins, including PuPuf4, APUM24, and ScPuf6, may contribute to their specific RNA-binding affinity due to its unique structural features. Given the conserved role of Puf4 in oomycete pathogenicity, we developed the first nano-material-free dsRNA delivery system via zoospore-specific uptake, effectively attenuating virulence in Pythium aphanidermatum and Ph. sojae through RNAi targeting Puf4. This study presents novel findings on structural and functional conservation of Puf4 and offers a promising RNAi-based strategy for controlling oomycete plant diseases.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.