{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Christensen PM"],"funding":["American Heart Association","Cecil and Ida Green Foundation","NIAID NIH HHS","National Institutes of Health","NIH HHS","NIGMS NIH HHS","National Science Foundation"],"pagination":["RP94929"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11630815"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["Bacterial membranes are complex and dynamic, arising from an array of evolutionary pressures. One enzyme that alters membrane compositions through covalent lipid modification is MprF. We recently identified that <i>Streptococcus agalactiae</i> MprF synthesizes lysyl-phosphatidylglycerol (Lys-PG) from anionic PG, and a novel cationic lipid, lysyl-glucosyl-diacylglycerol (Lys-Glc-DAG), from neutral glycolipid Glc-DAG. This unexpected result prompted us to investigate whether Lys-Glc-DAG occurs in other MprF-containing bacteria, and whether other novel MprF products exist. Here, we studied protein sequence features determining MprF substrate specificity. First, pairwise analyses identified several streptococcal MprFs synthesizing Lys-Glc-DAG. Second, a restricted Boltzmann machine-guided appr"],"journal":["eLife"],"pubmed_title":["Lipid discovery enabled by sequence statistics and machine learning."],"pmcid":["PMC11630815"],"funding_grant_id":["10.58275/AHA.23POST1013835.pc.gr.161273","R01 AI178692","R35 GM133631","R35GM133631","R01AI178692","MCB-1943442","R01 AI148366"],"pubmed_authors":["Uppuluri A","Morcos F","Guan Z","Christensen PM","Martin J","Joyce LR","Palmer KL","Wei Y"],"additional_accession":[]},"is_claimable":false,"name":"Lipid discovery enabled by sequence statistics and machine learning.","description":"Bacterial membranes are complex and dynamic, arising from an array of evolutionary pressures. One enzyme that alters membrane compositions through covalent lipid modification is MprF. We recently identified that <i>Streptococcus agalactiae</i> MprF synthesizes lysyl-phosphatidylglycerol (Lys-PG) from anionic PG, and a novel cationic lipid, lysyl-glucosyl-diacylglycerol (Lys-Glc-DAG), from neutral glycolipid Glc-DAG. This unexpected result prompted us to investigate whether Lys-Glc-DAG occurs in other MprF-containing bacteria, and whether other novel MprF products exist. Here, we studied protein sequence features determining MprF substrate specificity. First, pairwise analyses identified several streptococcal MprFs synthesizing Lys-Glc-DAG. Second, a restricted Boltzmann machine-guided appr","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-07-15T08:03:16.531Z","creation":"2025-04-19T14:36:49.657Z"},"accession":"S-EPMC11630815","cross_references":{"pubmed":["39656516"],"doi":["10.7554/eLife.94929"]}}