{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mao EYC"],"funding":["National Science and Technology Council of Taiwan"],"pagination":["4067-4078"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11040146"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["52(7)"],"pubmed_abstract":["Mitochondrial genome maintenance exonuclease 1 (MGME1) helps to ensure mitochondrial DNA (mtDNA) integrity by serving as an ancillary 5'-exonuclease for DNA polymerase γ. Curiously, MGME1 exhibits unique bidirectionality in vitro, being capable of degrading DNA from either the 5' or 3' end. The structural basis of this bidirectionally and, particularly, how it processes DNA from the 5' end to assist in mtDNA maintenance remain unclear. Here, we present a crystal structure of human MGME1 in complex with a 5'-overhang DNA, revealing that MGME1 functions as a rigid DNA clamp equipped with a single-strand (ss)-selective arch, allowing it to slide on single-stranded DNA in either the 5'-to-3' or 3'-to-5' direction. Using a nuclease activity assay, we have dissected the structural basis of MGME1"],"journal":["Nucleic acids research"],"pubmed_title":["Structural basis of how MGME1 processes DNA 5' ends to maintain mitochondrial genome integrity."],"pmcid":["PMC11040146"],"funding_grant_id":["MOST 110-2636-B-006-007"],"pubmed_authors":["Mao EYC","Wu CC","Yen HY"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of how MGME1 processes DNA 5' ends to maintain mitochondrial genome integrity.","description":"Mitochondrial genome maintenance exonuclease 1 (MGME1) helps to ensure mitochondrial DNA (mtDNA) integrity by serving as an ancillary 5'-exonuclease for DNA polymerase γ. Curiously, MGME1 exhibits unique bidirectionality in vitro, being capable of degrading DNA from either the 5' or 3' end. The structural basis of this bidirectionally and, particularly, how it processes DNA from the 5' end to assist in mtDNA maintenance remain unclear. Here, we present a crystal structure of human MGME1 in complex with a 5'-overhang DNA, revealing that MGME1 functions as a rigid DNA clamp equipped with a single-strand (ss)-selective arch, allowing it to slide on single-stranded DNA in either the 5'-to-3' or 3'-to-5' direction. Using a nuclease activity assay, we have dissected the structural basis of MGME1","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-06-02T01:43:19.198Z","creation":"2025-04-06T03:14:04.64Z"},"accession":"S-EPMC11040146","cross_references":{"pubmed":["38471810"],"doi":["10.1093/nar/gkae186"]}}