ArticleCell reports2026
A phosphohistidine phosphatase promotes starvation survival by dephosphorylating nucleoside diphosphate kinase.
Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Interaction of Bacterial Histidine Phosphatase SixA With Phosphocarrier Protein NPr and Phosphohistidine Analogs.Journal of molecular biology · 2026Article
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2 authors.
Funding
Abstract
Nucleoside diphosphate kinase (Ndk) is a ubiquitous enzyme that maintains the cellular nucleoside triphosphate (NTP) pool and participates in many other pathways of eukaryotes and prokaryotes. Here, we show that in Escherichia coli, Ndk is regulated by dephosphorylation of its phosphohistidine intermediate via the phosphatase SixA, thereby inhibiting nucleotide phosphoryl transfer activity. We further show that loss of this regulation alters the metabolic state of E. coli in low-nutrient conditions and reduces survival in long-term stationary phase. Similar regulation of Ndk by a phosphohistidine phosphatase has been reported previously for human cells, although the molecular interactions differ. The prevalence of SixA and Ndk orthologs in prokaryotes and the appearance of this regulatory mechanism in both E. coli and humans suggest that phosphohistidine phosphatase-mediated control of nucleoside diphosphate kinases may be widespread.
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