{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hollinger J"],"funding":["American Heart Association","NHLBI NIH HHS","Foundation for the National Institutes of Health","National Institutes of Health","NIGMS NIH HHS"],"pagination":["106322"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11143474"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["210"],"pubmed_abstract":["The protein Family with sequence similarity 210 member A (FAM210A) is a mitochondrial inner membrane protein that regulates the protein synthesis of mitochondrial DNA encoded genes. However, how it functions in this process is not well understood. Developing and optimizing a protein purification strategy will facilitate biochemical and structural studies of FAM210A. Here, we developed a method to purify human FAM210A with deleted mitochondrial targeting signal sequence using the MBP-His<sub>10</sub> fusion in Escherichia coli. The recombinant FAM210A protein was inserted into the E. coli cell membrane and purified from isolated bacterial cell membranes, followed by a two-step process using Ni-NTA resin-based immobilized-metal affinity chromatography (IMAC) and ion exchange purification. A "],"journal":["Protein expression and purification"],"pubmed_title":["Expression and purification of the mitochondrial transmembrane protein FAM210A in Escherichia coli."],"pmcid":["PMC11143474"],"funding_grant_id":["R35 GM133462","R01HL164584","R01 HL136432","R01HL169432","R35GM13346","R01HL132899","R01 HL132899","R01 HL164584","R01 HL147954","R01 HL169432","19POST34400013","R01HL147954","848985"],"pubmed_authors":["Wu J","Hollinger J","Yao P","Awayda KM","O'Connell MR"],"additional_accession":[]},"is_claimable":false,"name":"Expression and purification of the mitochondrial transmembrane protein FAM210A in Escherichia coli.","description":"The protein Family with sequence similarity 210 member A (FAM210A) is a mitochondrial inner membrane protein that regulates the protein synthesis of mitochondrial DNA encoded genes. However, how it functions in this process is not well understood. Developing and optimizing a protein purification strategy will facilitate biochemical and structural studies of FAM210A. Here, we developed a method to purify human FAM210A with deleted mitochondrial targeting signal sequence using the MBP-His<sub>10</sub> fusion in Escherichia coli. The recombinant FAM210A protein was inserted into the E. coli cell membrane and purified from isolated bacterial cell membranes, followed by a two-step process using Ni-NTA resin-based immobilized-metal affinity chromatography (IMAC) and ion exchange purification. A ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Oct","modification":"2026-06-02T06:54:31.969Z","creation":"2026-04-15T03:15:34.224Z"},"accession":"S-EPMC11143474","cross_references":{"pubmed":["37329934"],"doi":["10.1016/j.pep.2023.106322"]}}