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The exoribonuclease polynucleotide phosphorylase (PNPase), whose protein sequence is highly conserved across diverse species including humans, is crucial for RNA degradation and metabolism. In bacteria, PNPase and RNase E form multi-protein complexes with enzymes involved in glycolysis. A research team led by Dr. Sue Lin-Chao at the Institute of Molecular Biology, Academia Sinica, has established PNPase as a glycolytic metabolite sensor that links glycolysis to RNA degradation in Escherichia coli.

Their study demonstrates that a key glycolytic intermediate binds to and inhibits PNPase activity, likely facilitated by the close proximity of PNPase to glycolytic enzymes. This discovery establishes a molecular mechanism by which a glycolytic metabolite controls ribonuclease activity to regulate cellular RNA metabolism and gene expression. This regulatory system is likely utilized by other bacterial species relevant to human health, the environment, and industry, particularly those that rely on PNPase as their sole exoribonuclease.
The research was published in Nature Communications on August 13, 2026, with primary support from Academia Sinica.