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U.S.A."],"published-print":{"date-parts":[[2023,8]]},"abstract":"<jats:p>\n                    Recombination-promoting nuclease (Rpn) proteins are broadly distributed across bacterial phyla, yet their functions remain unclear. Here, we report that these proteins are toxin\u2013antitoxin systems, comprised of genes-within-genes, that combat phage infection. We show the small, highly variable Rpn\n                    <jats:italic>C<\/jats:italic>\n                    -terminal domains (Rpn\n                    <jats:sub>S<\/jats:sub>\n                    ), which are translated separately from the full-length proteins (Rpn\n                    <jats:sub>L<\/jats:sub>\n                    ), directly block the activities of the toxic Rpn\n                    <jats:sub>L<\/jats:sub>\n                    . The crystal structure of RpnA\n                    <jats:sub>S<\/jats:sub>\n                    revealed a dimerization interface encompassing \u03b1 helix that can have four amino acid repeats whose number varies widely among strains of the same species. Consistent with strong selection for the variation, we document that plasmid-encoded RpnP2\n                    <jats:sub>L<\/jats:sub>\n                    protects\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    against certain phages. We propose that many more intragenic-encoded proteins that serve regulatory roles remain to be discovered in all organisms.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2307382120","type":"journal-article","created":{"date-parts":[[2023,7,24]],"date-time":"2023-07-24T15:08:10Z","timestamp":1690211290000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":18,"title":["Toxic antiphage defense proteins inhibited by intragenic antitoxin proteins"],"prefix":"10.1073","volume":"120","author":[{"given":"Aoshu","family":"Zhong","sequence":"first","affiliation":[{"name":"Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaofang","family":"Jiang","sequence":"additional","affiliation":[{"name":"Intramural Research Program, National Library of Medicine, NIH, Bethesda, MD 20894"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alison B.","family":"Hickman","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katherine","family":"Klier","sequence":"additional","affiliation":[{"name":"Division of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriella I. 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