Xiaodi Liu , Xiangyu Zhu , Wenxin Jiang , Huanmin Du
{"title":"Identification and functional characterization of a potential l-Homoserine exporter in Corynebacterium glutamicum","authors":"Xiaodi Liu , Xiangyu Zhu , Wenxin Jiang , Huanmin Du","doi":"10.1016/j.engmic.2025.100240","DOIUrl":null,"url":null,"abstract":"<div><div>Exporter protein systems play a crucial role in the efficient production of valuable chemicals. However, the lack of active exporters significantly limits the application of industrial bio-based production, making the identification and utilization of novel exporters highly important. In this study, we discovered a novel <span>l</span>-Homoserine exporter, Cg0701, in <em>Corynebacterium glutamicum</em> through homology analysis. First, tolerance assays revealed that the <em>cg0701</em> overexpression strain (CgH-2) exhibited a 10.45% increase in cell growth compared to the control when cultivated with 30 g/L-Homoserine. Additionally, export assays demonstrated that the <span>l</span>-Homoserine export capacity of CgH-2 increased by approximately 30%. Furthermore, genomic overexpression of <em>cg0701</em> in an <span>l</span>-Homoserine-producing chassis also enhanced both tolerance and export activity. As a result, the recombinant strain CgH-11 produced 10.79 g/L-Homoserine in shake flask cultures and 48.72 g/L in a 5 L fermenter, representing improvements of 19.89% and 24.44%, respectively. In summary, our results indicate that Cg0701 is a novel <span>l</span>-Homoserine exporter in <em>C. glutamicum</em>, enriching our understanding of amino acid export systems and providing a valuable target for the construction of <span>l</span>-Homoserine microbial cell factories.</div></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"5 4","pages":"Article 100240"},"PeriodicalIF":0.0000,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Engineering Microbiology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2667370325000542","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Exporter protein systems play a crucial role in the efficient production of valuable chemicals. However, the lack of active exporters significantly limits the application of industrial bio-based production, making the identification and utilization of novel exporters highly important. In this study, we discovered a novel l-Homoserine exporter, Cg0701, in Corynebacterium glutamicum through homology analysis. First, tolerance assays revealed that the cg0701 overexpression strain (CgH-2) exhibited a 10.45% increase in cell growth compared to the control when cultivated with 30 g/L-Homoserine. Additionally, export assays demonstrated that the l-Homoserine export capacity of CgH-2 increased by approximately 30%. Furthermore, genomic overexpression of cg0701 in an l-Homoserine-producing chassis also enhanced both tolerance and export activity. As a result, the recombinant strain CgH-11 produced 10.79 g/L-Homoserine in shake flask cultures and 48.72 g/L in a 5 L fermenter, representing improvements of 19.89% and 24.44%, respectively. In summary, our results indicate that Cg0701 is a novel l-Homoserine exporter in C. glutamicum, enriching our understanding of amino acid export systems and providing a valuable target for the construction of l-Homoserine microbial cell factories.