{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T23:13:17Z","timestamp":1790809997046,"version":"4.1.0"},"reference-count":33,"publisher":"Elsevier BV","issue":"39","license":[{"start":{"date-parts":[[2018,9,1]],"date-time":"2018-09-01T00:00:00Z","timestamp":1535760000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,27]],"date-time":"2020-08-27T00:00:00Z","timestamp":1598486400000},"content-version":"vor","delay-in-days":726,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"HHS NIH National Institute of Neurological Disorders and Stroke (NINDS)","doi-asserted-by":"publisher","award":["1R01NS079965"],"award-info":[{"award-number":["1R01NS079965"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"HHS NIH National Institute on Aging (NIA)","doi-asserted-by":"publisher","award":["1R01AG036871"],"award-info":[{"award-number":["1R01AG036871"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000053","name":"HHS NIH National Eye Institute (NEI)","doi-asserted-by":"publisher","award":["5R01EY010804"],"award-info":[{"award-number":["5R01EY010804"]}],"id":[{"id":"10.13039\/100000053","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS NIH National Institute of General Medical Sciences (NIGMS)","doi-asserted-by":"publisher","award":["GM17151"],"award-info":[{"award-number":["GM17151"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2018,9]]},"DOI":"10.1074\/jbc.ra118.003838","type":"journal-article","created":{"date-parts":[[2018,8,7]],"date-time":"2018-08-07T18:35:11Z","timestamp":1533666911000},"page":"15021-15032","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":27,"title":["Mitochondrial methionyl N-formylation affects steady-state levels of oxidative phosphorylation complexes and their organization into supercomplexes"],"prefix":"10.1016","volume":"293","author":[{"given":"Tania","family":"Arguello","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caroline","family":"K\u00f6hrer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Uttam L.","family":"RajBhandary","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos T.","family":"Moraes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA118.003838_bib1","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1016\/j.bbagrm.2011.11.009","article-title":"Mechanism of protein biosynthesis in mammalian mitochondria","volume":"1819","author":"Christian","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA118.003838_bib2","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.biochi.2013.07.024","article-title":"Mitochondrial translation initiation machinery: conservation and diversification","volume":"100","author":"Kuzmenko","year":"2014","journal-title":"Biochimie"},{"key":"10.1074\/jbc.RA118.003838_bib3","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1128\/jb.176.3.547-552.1994","article-title":"Initiator transfer RNAs","volume":"176","author":"RajBhandary","year":"1994","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA118.003838_bib4","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s00441-016-2456-0","article-title":"The process of mammalian mitochondrial protein synthesis","volume":"367","author":"Mai","year":"2017","journal-title":"Cell Tissue Res"},{"key":"10.1074\/jbc.RA118.003838_bib5","doi-asserted-by":"crossref","first-page":"4294","DOI":"10.1128\/jb.174.13.4294-4301.1992","article-title":"Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli","volume":"174","author":"Guillon","year":"1992","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA118.003838_bib6","doi-asserted-by":"crossref","first-page":"15161","DOI":"10.1038\/s41598-017-15618-9","article-title":"The gene fmt, encoding tRNA(fMet)-formyl transferase, is essential for normal growth of M. bovis, but not for viability","volume":"7","author":"Vanunu","year":"2017","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.RA118.003838_bib7","doi-asserted-by":"crossref","first-page":"22143","DOI":"10.1074\/jbc.274.32.22143","article-title":"Formylation is not essential for initiation of protein synthesis in all eubacteria","volume":"274","author":"Newton","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.003838_bib8","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1128\/JB.182.10.2886-2892.2000","article-title":"Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA","volume":"182","author":"Li","year":"2000","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA118.003838_bib9","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.cmet.2011.07.010","article-title":"Mutations in MTFMT underlie a human disorder of formylation causing impaired mitochondrial translation","volume":"14","author":"Tucker","year":"2011","journal-title":"Cell Metab"},{"key":"10.1074\/jbc.RA118.003838_bib10","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/j.ymgme.2013.12.010","article-title":"Phenotypic spectrum of eleven patients and five novel MTFMT mutations identified by exome sequencing and candidate gene screening","volume":"111","author":"Haack","year":"2014","journal-title":"Mol. Genet. Metab"},{"key":"10.1074\/jbc.RA118.003838_bib11","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1136\/jmedgenet-2012-100846","article-title":"Molecular diagnosis in mitochondrial complex I deficiency using exome sequencing","volume":"49","author":"Haack","year":"2012","journal-title":"J. Med. Genet"},{"key":"10.1074\/jbc.RA118.003838_bib12","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/j.mito.2013.03.002","article-title":"Clinical and functional characterisation of the combined respiratory chain defect in two sisters due to autosomal recessive mutations in MTFMT","volume":"13","author":"Neeve","year":"2013","journal-title":"Mitochondrion"},{"key":"10.1074\/jbc.RA118.003838_bib13","doi-asserted-by":"crossref","first-page":"4103","DOI":"10.1093\/hmg\/ddv149","article-title":"An N-terminal formyl methionine on COX 1 is required for the assembly of cytochrome c oxidase","volume":"24","author":"Hinttala","year":"2015","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA118.003838_bib14","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1007\/s10048-016-0506-0","article-title":"Identification and functional characterization of a novel MTFMT mutation associated with selective vulnerability of the visual pathway and a mild neurological phenotype","volume":"18","author":"La Piana","year":"2017","journal-title":"Neurogenetics"},{"key":"10.1074\/jbc.RA118.003838_bib15","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1111\/petr.12758","article-title":"Challenges managing end-stage renal disease and kidney transplantation in a child with MTFMT mutation and moyamoya disease","volume":"20","author":"Oates","year":"2016","journal-title":"Pediatr. Transplant"},{"key":"10.1074\/jbc.RA118.003838_bib16","doi-asserted-by":"crossref","first-page":"32729","DOI":"10.1074\/jbc.M114.610626","article-title":"Biochemical characterization of pathogenic mutations in human mitochondrial methionyl-tRNA formyltransferase","volume":"289","author":"Sinha","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.003838_bib17","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1002\/dvg.22899","article-title":"Cre recombinase activity is inhibited in vivo but not ex vivo by a mutation in the asymmetric spacer region of the distal loxP site","volume":"53","author":"Arguello","year":"2015","journal-title":"Genesis"},{"key":"10.1074\/jbc.RA118.003838_bib18","doi-asserted-by":"crossref","first-page":"15085","DOI":"10.1074\/jbc.273.24.15085","article-title":"Mammalian mitochondrial methionyl-tRNA transformylase from bovine liver. Purification, characterization, and gene structure","volume":"273","author":"Takeuchi","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.003838_bib19","doi-asserted-by":"crossref","first-page":"20714","DOI":"10.1016\/S0021-9258(18)54767-0","article-title":"Initiation of protein synthesis in animal mitochondria. Purification and characterization of translational initiation factor 2","volume":"266","author":"Liao","year":"1991","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.003838_bib20","doi-asserted-by":"crossref","first-page":"5464","DOI":"10.1093\/nar\/gkh886","article-title":"Interaction of mitochondrial initiation factor 2 with mitochondrial fMet-tRNA","volume":"32","author":"Spencer","year":"2004","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA118.003838_bib21","doi-asserted-by":"crossref","first-page":"31774","DOI":"10.1074\/jbc.M304962200","article-title":"Mammalian mitochondrial initiation factor 2 supports yeast mitochondrial translation without formylated initiator tRNA","volume":"278","author":"Tibbetts","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA118.003838_bib22","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.it.2011.01.005","article-title":"Emerging role of damage-associated molecular patterns derived from mitochondria in inflammation","volume":"32","author":"Krysko","year":"2011","journal-title":"Trends Immunol"},{"key":"10.1074\/jbc.RA118.003838_bib23","doi-asserted-by":"crossref","first-page":"2486","DOI":"10.1002\/eji.200526338","article-title":"Human mitochondria-derived N-formylated peptides are novel agonists equally active on FPR and FPRL1, while Listeria monocytogenes-derived peptides preferentially activate FPR","volume":"35","author":"Rabiet","year":"2005","journal-title":"Eur. J. Immunol"},{"key":"10.1074\/jbc.RA118.003838_bib24","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/978-1-61779-504-6_14","article-title":"Radioactive labeling of mitochondrial translation products in cultured cells","volume":"837","author":"Sasarman","year":"2012","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/jbc.RA118.003838_bib25","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/S0091-679X(06)80028-2","article-title":"In vivo and in organello analyses of mitochondrial translation","volume":"80","author":"Fern\u00e1ndez-Silva","year":"2007","journal-title":"Methods Cell Biol"},{"key":"10.1074\/jbc.RA118.003838_bib26","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.bbabio.2013.12.009","article-title":"The function of the respiratory supercomplexes: the plasticity model","volume":"1837","author":"Acin-Perez","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA118.003838_bib27","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1016\/S1097-2765(04)00124-8","article-title":"Respiratory complex III is required to maintain complex I in mammalian mitochondria","volume":"13","author":"Ac\u00edn-P\u00e9rez","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA118.003838_bib28","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/j.molcel.2008.10.021","article-title":"Respiratory active mitochondrial supercomplexes","volume":"32","author":"Ac\u00edn-P\u00e9rez","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA118.003838_bib29","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/S0076-6879(08)04406-6","article-title":"Chapter 6 Mass spectrometric characterization of the thirteen subunits of bovine respiratory complexes that are encoded in mitochondrial DNA","volume":"456","author":"Walker","year":"2009","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA118.003838_bib30","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0076-6879(00)22022-3","article-title":"Nitrogen cavitation for cell disruption to obtain mitochondria from cultured cells","volume":"322","author":"Gottlieb","year":"2000","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA118.003838_bib31","doi-asserted-by":"crossref","DOI":"10.1002\/0471142905.hg1904s63","article-title":"Evaluation of the mitochondrial respiratory chain and oxidative phosphorylation system using blue native gel electrophoresis","author":"Diaz","year":"2009","journal-title":"Curr. Protoc. Hum. Genet"},{"key":"10.1074\/jbc.RA118.003838_bib32","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.ymeth.2007.10.006","article-title":"The many applications of acid urea polyacrylamide gel electrophoresis to studies of tRNAs and aminoacyl-tRNA synthetases","volume":"44","author":"K\u00f6hrer","year":"2008","journal-title":"Methods"},{"key":"10.1074\/jbc.RA118.003838_bib33","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/0005-2787(68)90185-8","article-title":"Cupric ion catalysis in hydrolysis of aminoacyl-tRNA","volume":"155","author":"Schofield","year":"1968","journal-title":"Biochim. Biophys. Acta"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820352820?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820352820?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA118.003838","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,18]],"date-time":"2021-12-18T13:14:50Z","timestamp":1639833290000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820352820"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,9]]},"references-count":33,"journal-issue":{"issue":"39","published-print":{"date-parts":[[2018,9]]}},"alternative-id":["S0021925820352820"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra118.003838","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2018,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mitochondrial methionyl N-formylation affects steady-state levels of oxidative phosphorylation complexes and their organization into supercomplexes","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA118.003838","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Arguello et al.","name":"copyright","label":"Copyright"}]}}