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dc.contributor.authorShahul Hameed, Umar F.
dc.contributor.authorSanislav, Oana
dc.contributor.authorLay, Sui T.
dc.contributor.authorAnnesley, Sarah J.
dc.contributor.authorJobichen, Chacko
dc.contributor.authorFisher, Paul R.
dc.contributor.authorSwaminathan, Kunchithapadam
dc.contributor.authorArold, Stefan T.
dc.date.accessioned2018-09-03T13:26:36Z
dc.date.available2018-09-03T13:26:36Z
dc.date.issued2018-08-24
dc.identifier.citationShahul Hameed UF, Sanislav O, Lay ST, Annesley SJ, Jobichen C, et al. (2018) Proteobacterial Origin of Protein Arginine Methylation and Regulation of Complex I Assembly by MidA. Cell Reports 24: 1996–2004. Available: http://dx.doi.org/10.1016/j.celrep.2018.07.075.
dc.identifier.issn2211-1247
dc.identifier.doi10.1016/j.celrep.2018.07.075
dc.identifier.urihttp://hdl.handle.net/10754/628476
dc.description.abstractThe human protein arginine methyltransferase NDUFAF7 controls the assembly of the ∼1-MDa mitochondrial complex I (CI; the NADH ubiquinone oxidoreductase) by methylating its subunit NDUFS2. We determined crystal structures of MidA, the Dictyostelium ortholog of NDUFAF7. The MidA catalytic core domain resembles other eukaryotic methyltransferases. However, three large core loops assemble into a regulatory domain that is likely to control ligand selection. Binding of MidA to NDUFS2 is weakened by methylation, suggesting a mechanism for methylation-controlled substrate release. Structural and bioinformatic analyses support that MidA and NDUFAF7 and their role in CI assembly are conserved from bacteria to humans, implying that protein methylation already existed in proteobacteria. In vivo studies confirmed the critical role of the MidA methyltransferase activity for CI assembly, growth, and phototaxis of Dictyostelium. Collectively, our data elucidate the origin of protein arginine methylation and its use by MidA/NDUFAF7 to regulate CI assembly.
dc.description.sponsorshipWe acknowledge SOLEIL for the provision of synchrotron radiation facilities, and we would like to thank L. Chavas, P. Legrand, S. Sirigu, and P. Montaville for assistance in using beamline PROXIMA 1; G. Fox, M. Savko, and B. Shepard for assistance in using beamline PROXIMA 2A; and J. Perez and A. Thureau for assistance in using the beamline SWING. We also acknowledge the National Synchrotron Radiation Research Centre beamline 13B1 of the Taiwan Synchrotron Facility for X-ray data collection. We thank the KAUST Bioscience Core Labs for their support. This research was supported by the King Abdullah University of Science and Technology (KAUST) and the Academic Research Fund (FRC) of the Ministry of Education, Singapore (to K.S.).
dc.publisherElsevier BV
dc.relation.urlhttps://www.sciencedirect.com/science/article/pii/S2211124718311938
dc.rightsThis is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectpost-translational modification
dc.subjectmethylation
dc.subjectSAXS
dc.subjectX-ray crystallography
dc.subjectSeahorse respirometry
dc.subjectcomplex I assembly
dc.subjectphototaxis
dc.subjectproteobacteria
dc.subjectevolution
dc.titleProteobacterial Origin of Protein Arginine Methylation and Regulation of Complex I Assembly by MidA
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.identifier.journalCell Reports
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDepartment of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.
dc.contributor.institutionDiscipline of Microbiology, La Trobe University, Plenty Rd., Bundoora, VIC 3086, Australia.
kaust.personShahul Hameed, Umar F.
kaust.personArold, Stefan T.
refterms.dateFOA2018-09-04T12:21:49Z
dc.date.published-online2018-08-24
dc.date.published-print2018-08


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This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Except where otherwise noted, this item's license is described as This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).