{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T13:02:18Z","timestamp":1790168538516,"version":"4.1.0"},"posted":{"date-parts":[[2026,9,18]]},"group-title":"Microbiology","reference-count":41,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T00:00:00Z","timestamp":1789689600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"award":["GM122506"],"award-info":[{"award-number":["GM122506"]}],"id":[{"id":"https:\/\/ror.org\/001d55x84","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,9,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>\n                  Inorganic polyphosphate (polyP) is a ubiquitous, multifunctional biomolecule that supports stress survival in bacteria. During nitrogen (N) starvation,\n                  <jats:italic>Escherichia coli<\/jats:italic>\n                  rapidly accumulates polyP, which drives the formation of RNA\u2013protein granules that sustain long-term survival. What triggers this upregulation has remained unknown. Here we show that polyamines, a group of highly conserved, amino acid-derived polycations, regulate polyP accumulation during N starvation. We found that deleting all nine polyamine biosynthesis genes elevates polyP during exponential growth and by more than 5-fold under N starvation, with shorter chains preferentially accumulating. To dissect which polyamine matters, we further deleted the three catabolic enzymes that consume polyamines as a nitrogen source, which enabled complementation assays. Supplying any one of the three physiological polyamines, putrescine, spermidine, or cadaverine, restored wild-type polyP levels during N starvation. We found that the absence of polyamines did not affect the steady-state levels of either the polyP-synthesizing kinase PPK or the exopolyphosphatase PPX, pointing instead to post-translational control of enzyme activity or to as-yet-unidentified polyamine-dependent regulators. These findings establish a direct metabolic link between two universal, functionally intertwined biomolecules and suggest that the polyamine decline upon N starvation contributes to the observed polyP accumulation.\n                <\/jats:p>","DOI":"10.64898\/2026.09.16.752086","type":"posted-content","created":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T05:35:17Z","timestamp":1789796117000},"source":"Crossref","is-referenced-by-count":0,"title":["Polyamines control inorganic polyphosphate levels during bacterial nitrogen starvation"],"prefix":"10.64898","author":[{"given":"Jian","family":"Guan","sequence":"first","affiliation":[{"name":"Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 49109"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavithra","family":"Mahadevan","sequence":"additional","affiliation":[{"name":"Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 49109"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ursula","family":"Jakob","sequence":"additional","affiliation":[{"name":"Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 49109"},{"name":"Department of Biological Chemistry, Michigan Medicine, Ann Arbor, MI, 48109"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"54368","reference":[{"key":"2026092305150509000_2026.09.16.752086v1.1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.REV118.002808"},{"key":"2026092305150509000_2026.09.16.752086v1.2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.R116.734780"},{"key":"2026092305150509000_2026.09.16.752086v1.3","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2006.05103.x"},{"key":"2026092305150509000_2026.09.16.752086v1.4","doi-asserted-by":"crossref","first-page":"2112","DOI":"10.1016\/S0021-9258(18)69373-1","article-title":"Polyamines and Ribosome Structure","volume":"235","year":"1960","journal-title":"Journal of Biological Chemistry"},{"key":"2026092305150509000_2026.09.16.752086v1.5","doi-asserted-by":"crossref","unstructured":"Baijal K , Kore B , Abramchuk I , Denoncourt A , Han SA , Simms A , Dagenais A , Long AR , Rudner AD , Lavallee-Adam M , Gray MJ , Downey M. 2025. Identification of polyphosphate-binding proteins in Escherichia coli uncovers targets involved in translation control and ribosome biogenesis. 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