{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMRM2, also known as FTSJ2, functions as a mitochondrial RNA methyltransferase that catalyzes the 2′-O‐methyl modification of specific residues in the mitochondrial 16S rRNA. This modification, which occurs at residue U1369 in the peptidyl transferase center of the mitoribosome, is critical for the proper assembly of the mitochondrial large ribosomal subunit and for efficient mitochondrial translation. Dysfunction of this enzymatic activity disrupts rRNA maturation, thereby impairing ribosome formation and respiratory competence."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nLoss of function or pathogenic mutations in MRM2 have been linked to human mitochondrial disease. For instance, a missense mutation in MRM2 was identified in a patient displaying a MELAS‐like phenotype, where defective 2′-O-methyl modification in 16S rRNA correlated with impaired mitochondrial translation and respiratory chain deficiencies. These findings underscore the enzyme’s essential role in maintaining mitochondrial function and highlight its relevance to mitochondrial encephalomyopathies."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies on the FTSJ2 gene further confirm its evolutionary conservation and its dual functions; while it shares significant homology with bacterial rRNA methyltransferases, it also exhibits characteristics of a stress‐responsive heat shock protein. In mammalian cells, FTSJ2 is localized to the mitochondria and displays regulatory behavior under stress conditions, with emerging evidence also suggesting a potential role in modulating cellular invasiveness in certain cancer types."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joanna Rorbach, Pierre Boesch, Payam A Gammage, et al. "}, {"type": "b", "children": [{"type": "t", "text": "MRM2 and MRM3 are involved in biogenesis of the large subunit of the mitochondrial ribosome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.E14-01-0014"}], "href": "https://doi.org/10.1091/mbc.E14-01-0014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25009282"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25009282"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Ken-Wing Lee, Daniel F Bogenhagen "}, {"type": "b", "children": [{"type": "t", "text": "Assignment of 2'-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.C114.581868"}], "href": "https://doi.org/10.1074/jbc.C114.581868"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25074936"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25074936"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Caterina Garone, Aaron R D'Souza, Cristina Dallabona, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Defective mitochondrial rRNA methyltransferase MRM2 causes MELAS-like clinical syndrome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddx314"}], "href": "https://doi.org/10.1093/hmg/ddx314"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28973171"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28973171"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Yick-Pang Ching, Hai-Jun Zhou, Jian-Gang Yuan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification and characterization of FTSJ2, a novel human nucleolar protein homologous to bacterial ribosomal RNA methyltransferase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genomics (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1006/geno.2001.6670"}], "href": "https://doi.org/10.1006/geno.2001.6670"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11827451"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11827451"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Cheng-Wei Lai, Hsiao-Ling Chen, Ken-Yo Lin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "FTSJ2, a heat shock-inducible mitochondrial protein, suppresses cell invasion and migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0090818"}], "href": "https://doi.org/10.1371/journal.pone.0090818"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24595062"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24595062"}]}]}]}