{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T12:06:28Z","timestamp":1789560388935,"version":"build-2803163510"},"posted":{"date-parts":[[2026,9,11]]},"group-title":"Molecular Biology","reference-count":48,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T00:00:00Z","timestamp":1789084800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"name":"NIH","award":["R01HL149450"],"award-info":[{"award-number":["R01HL149450"]}]},{"name":"NIH","award":["R21AI153660"],"award-info":[{"award-number":["R21AI153660"]}]},{"name":"NIH","award":["R21AI144748"],"award-info":[{"award-number":["R21AI144748"]}]},{"name":"NIH","award":["R01AI140472"],"award-info":[{"award-number":["R01AI140472"]}]},{"name":"Pittsfield Anti-Tuberculosis Association"},{"name":"National Research Service","award":["GM008515"],"award-info":[{"award-number":["GM008515"]}]},{"name":"National Research Service","award":["GM139789"],"award-info":[{"award-number":["GM139789"]}]},{"name":"Science Without Borders from CAPES-Brazil","award":["0328-13-8"],"award-info":[{"award-number":["0328-13-8"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,9,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>\n                  Maintenance of membrane integrity and proton motive force (PMF) is critical for bacterial survival. The phage shock protein (Psp) system, conserved across bacterial species, stabilizes the membrane, maintains PMF, and protects against envelope damage. However, how the conserved effector PspA contributes to PMF maintenance remains unclear. Here, using the mycobacterial Psp system as a genetically tractable model, we provide mechanistic insight into this process. We show that PspA and the accessory protein PspM jointly sustain membrane potential, with PspM required to maintain a \u223c70 kDa PspA isoform at the membrane during envelope stress. Loss of PspA increases susceptibility to thioridazine, which targets type II NADH dehydrogenase (NDH-2), and to Ro 48-8071, an inhibitor of menaquinone biosynthesis. Notably, hypersusceptibility to thioridazine is rescued by exogenous menaquinone. Consistent with these phenotypes, a\n                  <jats:italic>pspA<\/jats:italic>\n                  -deficient mutant exhibits impaired NADH dehydrogenase activity despite unchanged abundance of NDH-2 and menaquinone (MK-9). Together, these findings identify a functional link between PspA and NADH dehydrogenase-dependent respiration and suggest that PspA contributes to PMF maintenance by supporting respiratory electron transfer.\n                <\/jats:p>","DOI":"10.64898\/2026.09.09.750162","type":"posted-content","created":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T15:55:29Z","timestamp":1789142129000},"source":"Crossref","is-referenced-by-count":0,"title":["The phage shock protein A (PspA) maintains membrane potential and supports NADH dehydrogenase function in mycobacteria"],"prefix":"10.64898","author":[{"given":"Pratik","family":"Datta","sequence":"first","affiliation":[{"name":"Public Health Research Institute, Rutgers New Jersey Medical School, Rutgers Biomedical and Health Sciences, Newark, NJ 07103"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberta","family":"Provvedi","sequence":"additional","affiliation":[{"name":"Department of Molecular Medicine, University of 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