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A critical factor for elevated levels of labile iron is the overt accumulation of nuclear receptor coactivator 4 (NCOA4), which promotes autophagic degradation of ferritin in a process termed ferritinophagy. Here, we identify a novel post-translational modification on NCOA4 that is essential for its interaction with ferritin in the iron-replete condition of Mtb-infected cells. Specifically, protein arginine methyltransferase 5 (PRMT5) confers symmetric dimethylation on NCOA4, which promotes ferritinophagy-mediated ferroptosis. Using loss-of-function studies, we show that PRMT5 is required for lipid peroxidation, bacterial survival, and dissemination in Mtb-infected mice. Additionally, the overexpression of a methylation-deficient mutant of NCOA4 phenocopies the depletion of PRMT5 and reduces ferritinophagy in Mtb-infected cells. Mechanistically, we identify that PRMT5-mediated methylation enhances the cytoplasmic retention of NCOA4 and reduces its nuclear availability. Thus, our findings uncover the key interaction between NCOA4 and ferritin that regulates ferroptosis and mycobacterial survival during infection. Perturbation of this interaction results in reduced Mtb loads and alleviated disease pathology.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1014614","type":"journal-article","created":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T17:37:38Z","timestamp":1790098658000},"page":"e1014614","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Role of PRMT5 in regulating ferritinophagy during Mycobacterium tuberculosis infection"],"prefix":"10.1371","volume":"22","author":[{"given":"Smriti","family":"Sundar","sequence":"first","affiliation":[{"name":"Indian Institute of Science","place":["Bengaluru, Karnataka, India"],"department":["Department of Microbiology and Cell Biology"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raju S.","family":"Rajmani","sequence":"additional","affiliation":[{"name":"Indian Institute of Science","place":["Bengaluru, Karnataka, India"],"department":["Molecular Biophysics Unit"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0006-5707","authenticated-orcid":true,"given":"Kithiganahalli Narayanaswamy","family":"Balaji","sequence":"additional","affiliation":[{"name":"Indian Institute of Science","place":["Bengaluru, Karnataka, India"],"department":["Department of Microbiology and Cell Biology"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2026,9,22]]},"reference":[{"issue":"3","key":"ppat.1014614.ref001","doi-asserted-by":"crossref","DOI":"10.1128\/microbiolspec.TBTB2-0030-2016","article-title":"Mycobacterium tuberculosis in the face of host-imposed nutrient limitation","volume":"5","author":"M Berney","year":"2017","journal-title":"Microbiol Spectr"},{"issue":"10","key":"ppat.1014614.ref002","doi-asserted-by":"crossref","first-page":"6788","DOI":"10.1074\/jbc.M112.445056","article-title":"Intracellular Mycobacterium tuberculosis exploits host-derived fatty acids to limit metabolic stress","volume":"288","author":"W Lee","year":"2013","journal-title":"J Biol Chem"},{"issue":"11","key":"ppat.1014614.ref003","doi-asserted-by":"crossref","first-page":"4376","DOI":"10.1073\/pnas.0711159105","article-title":"Mycobacterial persistence requires the utilization of host cholesterol","volume":"105","author":"AK Pandey","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"12","key":"ppat.1014614.ref004","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1086\/518040","article-title":"The effect of the host\u2019s iron status on tuberculosis","volume":"195","author":"JR Boelaert","year":"2007","journal-title":"J Infect Dis"},{"issue":"3","key":"ppat.1014614.ref005","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S1386-6532(00)00136-0","article-title":"Iron and Mycobacterium tuberculosis infection","volume":"20","author":"N Lounis","year":"2001","journal-title":"J Clin Virol"},{"issue":"8","key":"ppat.1014614.ref006","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S0966-842X(01)02098-4","article-title":"Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions","volume":"9","author":"JR Forbes","year":"2001","journal-title":"Trends Microbiol"},{"issue":"8","key":"ppat.1014614.ref007","doi-asserted-by":"crossref","first-page":"3470","DOI":"10.1182\/blood.V87.8.3470.bloodjournal8783470","article-title":"Associations of iron overload in Africa with hepatocellular carcinoma and tuberculosis: Strachan\u2019s 1929 thesis revisited","volume":"87","author":"VR Gordeuk","year":"1996","journal-title":"Blood"},{"issue":"1","key":"ppat.1014614.ref008","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1189\/jlb.0606405","article-title":"Hereditary hemochromatosis results in decreased iron acquisition and growth by Mycobacterium tuberculosis within human 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