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Our research on\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. methanolicus<\/jats:italic>\n                    <\/jats:styled-content>\n                    MGA3 identifies its MscS as the sole mechanosensitive channel in this organism and a key exporter of the amino acid\n                    <jats:sc>l<\/jats:sc>\n                    \u2010glutamate, providing valuable insights into its potential for industrial applications. Transcriptomic analysis of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. methanolicus<\/jats:italic>\n                    <\/jats:styled-content>\n                    wild type cultured on an\n                    <jats:sc>l<\/jats:sc>\n                    \u2010glutamate production medium revealed downregulation of the fatty acid biosynthesis genes\n                    <jats:italic>fadR<\/jats:italic>\n                    ,\n                    <jats:italic>fadF<\/jats:italic>\n                    ,\n                    <jats:italic>mutB2<\/jats:italic>\n                    , and\n                    <jats:italic>acdA<\/jats:italic>\n                    , suggesting that fatty acid metabolism is influenced by\n                    <jats:sc>l<\/jats:sc>\n                    \u2010glutamate overproduction, with consequent changes in membrane fluidity likely driving mechanosensitive channel\u2010mediated\n                    <jats:sc>l<\/jats:sc>\n                    \u2010glutamate efflux. The MscS\u2010like channel in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. methanolicus<\/jats:italic>\n                    <\/jats:styled-content>\n                    shares structural and functional similarities with MscS in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Escherichia coli<\/jats:italic>\n                    <\/jats:styled-content>\n                    and with MscCG in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>Corynebacterium glutamicum<\/jats:italic>\n                    <\/jats:styled-content>\n                    .\n                    <jats:italic>In silico<\/jats:italic>\n                    structural predictions show that MGA3 MscS forms a homoheptameric structure with a transmembrane TM\u2010barrel, resembling that of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>E. coli<\/jats:italic>\n                    <\/jats:styled-content>\n                    MscS. The opening mechanism of the channel, driven by membrane dynamics, involves coordinated rotation and flipping of its transmembrane helices, with variations in lipid composition potentially influencing the channel's activity. Additionally, under biotin\u2010replete conditions, where this essential coenzyme supports carboxylases involved in fatty acid biosynthesis,\n                    <jats:sc>l<\/jats:sc>\n                    \u2010glutamate overproduction was suppressed in MGA3. Finally, metabolic engineering experiments inducing MscS gain\u2010 and loss\u2010of\u2010function further confirmed the channel's critical role in\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. methanolicus<\/jats:italic>\n                    <\/jats:styled-content>\n                    amino acid production, proportionally enhancing and reducing\n                    <jats:sc>l<\/jats:sc>\n                    \u2010glutamate efflux, respectively. These findings open doors to novel strategies for engineering\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>B. methanolicus<\/jats:italic>\n                    <\/jats:styled-content>\n                    and related methylotrophic organisms for sustainable amino acid production.\n                  <\/jats:p>","DOI":"10.1111\/1751-7915.70252","type":"journal-article","created":{"date-parts":[[2025,10,22]],"date-time":"2025-10-22T10:41:56Z","timestamp":1761129716000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Identification of MscS as a Key L\u2010Glutamate Exporter in\n                    <i>Bacillus methanolicus<\/i>"],"prefix":"10.1111","volume":"18","author":[{"given":"Luciana Fernandes","family":"Brito","sequence":"first","affiliation":[{"name":"Department of Biotechnology and Food Science Norwegian University of Science and Technology  Trondheim Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Davide","family":"Luciano","sequence":"additional","affiliation":[{"name":"Department of Biotechnology and Food Science Norwegian University of Science and Technology  Trondheim Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7097-6656","authenticated-orcid":false,"given":"Marta","family":"Irla","sequence":"additional","affiliation":[{"name":"Department of Biological and Chemical Engineering Aarhus University  Aarhus Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Virant","sequence":"additional","affiliation":[{"name":"Acies Bio d.o.o.  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