NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial, also knowns as NADH-ubiquinone oxidoreductase 20 kDa subunit, Complex I-20kD (CI-20kD), or PSST subunit is an enzyme that in humans is encoded by the NDUFS7gene.[5][6][7] The NDUFS7 protein is a subunit of NADH dehydrogenase (ubiquinone) also known as Complex I, which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.[8]
The NDUFS7 gene is located on the p arm of chromosome 19 in position 13.3.[6] The NDUFS7 gene produces a 25 kDa protein composed of 238 amino acids.[9][10] The PSST subunit is highly conserved across evolutionary distances. Crystal structures and mutational studies indicate that it is one of the ubiquinone binding sites of Complex I, together with the TYKY (NDUFS8) subunit.[11] It has been proposed that PSST, along with TYKY, 49 kDa, ND1 and ND5 subunits interact with iron-sulfur clusters as part of the catalytic core of NADH dehydrogenase (ubiquinone).[12]
Functionedit
The PSST subunit encoded by the NDUSF7 gene is one of over 40 subunits involved in the transfer of electrons from NADH to ubiquinone. Specifically, it is thought that the PSST subunit directly couples electron transfer between the iron-sulfur cluster N2 and ubiquinone, along with ubiquinone-binding ND1.[12] Functional evidence for the importance of PSST has been garnered from mutational studies in the obligate aerobic yeast, Yarrow lipolytic, which elucidated a central role in proton translocation that was reduced in mutant forms of the subunit.[13]
Clinical Significanceedit
Mitochondrial complex I deficiency (MT-C1D) is caused by mutations affecting the NDUFS7 gene. Complex I deficiency is a disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations, from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber's hereditary optic neuropathy, and some forms of Parkinson's disease. Leigh syndrome is an early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord, and is the most common mitochondrial encephalomyopathy. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, dysphagia, and lactic acidosis.[14][7][15]
Interactionsedit
In addition to co-subunits for complex I, NDUFS7 has protein-protein interactions with ENO2 and ARRB2.[16][17]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000115286 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000020153 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Hyslop SJ, Duncan AM, Pitkänen S, Robinson BH (November 1996). "Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13". Genomics. 37 (3): 375–80. doi:10.1006/geno.1996.0572. PMID 8938450.
^Donald Voet; Judith G. Voet; Charlotte W. Pratt (2013). "18". Fundamentals of biochemistry : life at the molecular level (4th ed.). Hoboken, NJ: Wiley. pp. 581–620. ISBN9780470547847.
^Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC4076475. PMID 23965338.
^"NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).
^Angerer H, Nasiri HR, Niedergesäß V, Kerscher S, Schwalbe H, Brandt U (October 2012). "Tracing the tail of ubiquinone in mitochondrial complex I". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817 (10): 1776–84. doi:10.1016/j.bbabio.2012.03.021. PMID 22484275.
^ abSchuler, Franz; Casida, John E. (2001-07-02). "Functional coupling of PSST and ND1 subunits in NADH:ubiquinone oxidoreductase established by photoaffinity labeling". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1506 (1): 79–87. doi:10.1016/S0005-2728(01)00183-9. ISSN 0005-2728. PMID 11418099.
^Ahlers PM, Zwicker K, Kerscher S, Brandt U (August 2000). "Function of conserved acidic residues in the PSST homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica" (PDF). The Journal of Biological Chemistry. 275 (31): 23577–82. doi:10.1074/jbc.M002074200. PMID 10811805.
^Smeitink J, van den Heuvel L (June 1999). "Human mitochondrial complex I in health and disease". American Journal of Human Genetics. 64 (6): 1505–10. doi:10.1086/302432. PMC1377894. PMID 10330338.
^Triepels RH, van den Heuvel LP, Loeffen JL, Buskens CA, Smeets RJ, Rubio Gozalbo ME, Budde SM, Mariman EC, Wijburg FA, Barth PG, Trijbels JM, Smeitink JA (June 1999). "Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear encoded subunit of complex I" (PDF). Annals of Neurology. 45 (6): 787–90. doi:10.1002/1531-8249(199906)45:6<787::AID-ANA13>3.0.CO;2-6. PMID 10360771. S2CID 10547092.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA (December 1998). "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochemical and Biophysical Research Communications. 253 (2): 415–22. doi:10.1006/bbrc.1998.9786. PMID 9878551.
Triepels RH, Hanson BJ, van den Heuvel LP, Sundell L, Marusich MF, Smeitink JA, Capaldi RA (March 2001). "Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns". The Journal of Biological Chemistry. 276 (12): 8892–7. doi:10.1074/jbc.M009903200. hdl:2066/185667. PMID 11112787.
Schuler F, Casida JE (July 2001). "Functional coupling of PSST and ND1 subunits in NADH:ubiquinone oxidoreductase established by photoaffinity labeling". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1506 (1): 79–87. doi:10.1016/S0005-2728(01)00183-9. PMID 11418099.
Ugalde C, Janssen RJ, van den Heuvel LP, Smeitink JA, Nijtmans LG (March 2004). "Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency". Human Molecular Genetics. 13 (6): 659–67. doi:10.1093/hmg/ddh071. PMID 14749350.
Ricci JE, Muñoz-Pinedo C, Fitzgerald P, Bailly-Maitre B, Perkins GA, Yadava N, Scheffler IE, Ellisman MH, Green DR (June 2004). "Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain". Cell. 117 (6): 773–86. doi:10.1016/j.cell.2004.05.008. PMID 15186778. S2CID 14016847.
Lebon S, Rodriguez D, Bridoux D, Zerrad A, Rötig A, Munnich A, Legrand A, Slama A (April 2007). "A novel mutation in the human complex I NDUFS7 subunit associated with Leigh syndrome". Molecular Genetics and Metabolism. 90 (4): 379–82. doi:10.1016/j.ymgme.2006.12.007. PMID 17275378.
Lebon S, Minai L, Chretien D, Corcos J, Serre V, Kadhom N, Steffann J, Pauchard JY, Munnich A, Bonnefont JP, Rötig A (2007). "A novel mutation of the NDUFS7 gene leads to activation of a cryptic exon and impaired assembly of mitochondrial complex I in a patient with Leigh syndrome". Molecular Genetics and Metabolism. 92 (1–2): 104–8. doi:10.1016/j.ymgme.2007.05.010. PMID 17604671.
April 12, 2024
ndufs7, nadh, dehydrogenase, ubiquinone, iron, sulfur, protein, mitochondrial, also, knowns, nadh, ubiquinone, oxidoreductase, subunit, complex, 20kd, 20kd, psst, subunit, enzyme, that, humans, encoded, gene, protein, subunit, nadh, dehydrogenase, ubiquinone, . NADH dehydrogenase ubiquinone iron sulfur protein 7 mitochondrial also knowns as NADH ubiquinone oxidoreductase 20 kDa subunit Complex I 20kD CI 20kD or PSST subunit is an enzyme that in humans is encoded by the NDUFS7 gene 5 6 7 The NDUFS7 protein is a subunit of NADH dehydrogenase ubiquinone also known as Complex I which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain 8 NDUFS7IdentifiersAliasesNDUFS7 CI 20 CI 20KD MY017 PSST NADH ubiquinone oxidoreductase core subunit S7 MC1DN3External IDsOMIM 601825 MGI 1922656 HomoloGene 11535 GeneCards NDUFS7Gene location Human Chr Chromosome 19 human 1 Band19p13 3Start1 383 527 bp 1 End1 395 589 bp 1 Gene location Mouse Chr Chromosome 10 mouse 2 Band10 C1 10 39 72 cMStart80 084 955 bp 2 End80 092 628 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed ingastrocnemius muscleleft ventricleright adrenal glandanterior pituitarytriceps brachii muscleleft adrenal glandbody of stomachvastus lateralis muscleBrodmann area 9right lobe of liverTop expressed ininterventricular septumfacial motor nucleusmyocardium of ventricledigastric muscleextraocular musclesoleus musclethoracic diaphragmcardiac musclesright ventriclemasseter muscleMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular function4 iron 4 sulfur cluster binding quinone binding iron sulfur cluster binding metal ion binding oxidoreductase activity acting on NAD P H quinone or similar compound as acceptor protein binding oxidoreductase activity NADH dehydrogenase activity NADH dehydrogenase ubiquinone activity protease bindingCellular componentsynaptic membrane neuronal cell body mitochondrial matrix mitochondrion neuron projection respirasome mitochondrial respiratory chain complex IBiological processmitochondrial respiratory chain complex I assembly mitochondrial electron transport NADH to ubiquinone aerobic respiration electron transport coupled proton transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez37429175406EnsemblENSG00000115286ENSMUSG00000020153UniProtO75251Q9DC70RefSeq mRNA NM 024407NM 001363602NM 029272NM 001364694RefSeq protein NP 077718NP 001350531NP 083548NP 001351623Location UCSC Chr 19 1 38 1 4 MbChr 10 80 08 80 09 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Structure 2 Function 3 Clinical Significance 4 Interactions 5 References 6 Further readingStructure editThe NDUFS7 gene is located on the p arm of chromosome 19 in position 13 3 6 The NDUFS7 gene produces a 25 kDa protein composed of 238 amino acids 9 10 The PSST subunit is highly conserved across evolutionary distances Crystal structures and mutational studies indicate that it is one of the ubiquinone binding sites of Complex I together with the TYKY NDUFS8 subunit 11 It has been proposed that PSST along with TYKY 49 kDa ND1 and ND5 subunits interact with iron sulfur clusters as part of the catalytic core of NADH dehydrogenase ubiquinone 12 Function editThe PSST subunit encoded by the NDUSF7 gene is one of over 40 subunits involved in the transfer of electrons from NADH to ubiquinone Specifically it is thought that the PSST subunit directly couples electron transfer between the iron sulfur cluster N2 and ubiquinone along with ubiquinone binding ND1 12 Functional evidence for the importance of PSST has been garnered from mutational studies in the obligate aerobic yeast Yarrow lipolytic which elucidated a central role in proton translocation that was reduced in mutant forms of the subunit 13 Clinical Significance editMitochondrial complex I deficiency MT C1D is caused by mutations affecting the NDUFS7 gene Complex I deficiency is a disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult onset neurodegenerative disorders Phenotypes include macrocephaly with progressive leukodystrophy non specific encephalopathy cardiomyopathy myopathy liver disease Leigh syndrome Leber s hereditary optic neuropathy and some forms of Parkinson s disease Leigh syndrome is an early onset progressive neurodegenerative disorder characterized by the presence of focal bilateral lesions in one or more areas of the central nervous system including the brainstem thalamus basal ganglia cerebellum and spinal cord and is the most common mitochondrial encephalomyopathy Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation hypotonia ataxia weakness vision loss eye movement abnormalities seizures dysphagia and lactic acidosis 14 7 15 Interactions editIn addition to co subunits for complex I NDUFS7 has protein protein interactions with ENO2 and ARRB2 16 17 References edit a b c GRCh38 Ensembl release 89 ENSG00000115286 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000020153 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Hyslop SJ Duncan AM Pitkanen S Robinson BH November 1996 Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13 Genomics 37 3 375 80 doi 10 1006 geno 1996 0572 PMID 8938450 a b Entrez Gene NDUFS7 NADH dehydrogenase ubiquinone Fe S protein 7 20kDa NADH coenzyme Q reductase a b NDUFS7 NADH dehydrogenase ubiquinone iron sulfur protein 7 mitochondrial precursor Homo sapiens Human NDUFS7 gene amp protein www uniprot org Retrieved 2018 07 18 Donald Voet Judith G Voet Charlotte W Pratt 2013 18 Fundamentals of biochemistry life at the molecular level 4th ed Hoboken NJ Wiley pp 581 620 ISBN 9780470547847 Zong NC Li H Li H Lam MP Jimenez RC Kim CS Deng N Kim AK Choi JH Zelaya I Liem D Meyer D Odeberg J Fang C Lu HJ Xu T Weiss J Duan H Uhlen M Yates JR Apweiler R Ge J Hermjakob H Ping P Oct 2013 Integration of cardiac proteome biology and medicine by a specialized knowledgebase Circulation Research 113 9 1043 53 doi 10 1161 CIRCRESAHA 113 301151 PMC 4076475 PMID 23965338 NADH dehydrogenase ubiquinone iron sulfur protein 7 mitochondrial Cardiac Organellar Protein Atlas Knowledgebase COPaKB Angerer H Nasiri HR Niedergesass V Kerscher S Schwalbe H Brandt U October 2012 Tracing the tail of ubiquinone in mitochondrial complex I Biochimica et Biophysica Acta BBA Bioenergetics 1817 10 1776 84 doi 10 1016 j bbabio 2012 03 021 PMID 22484275 a b Schuler Franz Casida John E 2001 07 02 Functional coupling of PSST and ND1 subunits in NADH ubiquinone oxidoreductase established by photoaffinity labeling Biochimica et Biophysica Acta BBA Bioenergetics 1506 1 79 87 doi 10 1016 S0005 2728 01 00183 9 ISSN 0005 2728 PMID 11418099 Ahlers PM Zwicker K Kerscher S Brandt U August 2000 Function of conserved acidic residues in the PSST homologue of complex I NADH ubiquinone oxidoreductase from Yarrowia lipolytica PDF The Journal of Biological Chemistry 275 31 23577 82 doi 10 1074 jbc M002074200 PMID 10811805 Smeitink J van den Heuvel L June 1999 Human mitochondrial complex I in health and disease American Journal of Human Genetics 64 6 1505 10 doi 10 1086 302432 PMC 1377894 PMID 10330338 Triepels RH van den Heuvel LP Loeffen JL Buskens CA Smeets RJ Rubio Gozalbo ME Budde SM Mariman EC Wijburg FA Barth PG Trijbels JM Smeitink JA June 1999 Leigh syndrome associated with a mutation in the NDUFS7 PSST nuclear encoded subunit of complex I PDF Annals of Neurology 45 6 787 90 doi 10 1002 1531 8249 199906 45 6 lt 787 AID ANA13 gt 3 0 CO 2 6 PMID 10360771 S2CID 10547092 Interaction Details IntAct Molecular Interaction Database Interaction Details IntAct Molecular Interaction Database Further reading editMaruyama K Sugano S January 1994 Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides Gene 138 1 2 171 4 doi 10 1016 0378 1119 94 90802 8 PMID 8125298 Suzuki Y Yoshitomo Nakagawa K Maruyama K Suyama A Sugano S October 1997 Construction and characterization of a full length enriched and a 5 end enriched cDNA library Gene 200 1 2 149 56 doi 10 1016 S0378 1119 97 00411 3 PMID 9373149 Loeffen JL Triepels RH van den Heuvel LP Schuelke M Buskens CA Smeets RJ Trijbels JM Smeitink JA December 1998 cDNA of eight nuclear encoded subunits of NADH ubiquinone oxidoreductase human complex I cDNA characterization completed Biochemical and Biophysical Research Communications 253 2 415 22 doi 10 1006 bbrc 1998 9786 PMID 9878551 Triepels RH Hanson BJ van den Heuvel LP Sundell L Marusich MF Smeitink JA Capaldi RA March 2001 Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns The Journal of Biological Chemistry 276 12 8892 7 doi 10 1074 jbc M009903200 hdl 2066 185667 PMID 11112787 Schuler F Casida JE July 2001 Functional coupling of PSST and ND1 subunits in NADH ubiquinone oxidoreductase established by photoaffinity labeling Biochimica et Biophysica Acta BBA Bioenergetics 1506 1 79 87 doi 10 1016 S0005 2728 01 00183 9 PMID 11418099 Ugalde C Janssen RJ van den Heuvel LP Smeitink JA Nijtmans LG March 2004 Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency Human Molecular Genetics 13 6 659 67 doi 10 1093 hmg ddh071 PMID 14749350 Ricci JE Munoz Pinedo C Fitzgerald P Bailly Maitre B Perkins GA Yadava N Scheffler IE Ellisman MH Green DR June 2004 Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain Cell 117 6 773 86 doi 10 1016 j cell 2004 05 008 PMID 15186778 S2CID 14016847 Lebon S Rodriguez D Bridoux D Zerrad A Rotig A Munnich A Legrand A Slama A April 2007 A novel mutation in the human complex I NDUFS7 subunit associated with Leigh syndrome Molecular Genetics and Metabolism 90 4 379 82 doi 10 1016 j ymgme 2006 12 007 PMID 17275378 Lebon S Minai L Chretien D Corcos J Serre V Kadhom N Steffann J Pauchard JY Munnich A Bonnefont JP Rotig A 2007 A novel mutation of the NDUFS7 gene leads to activation of a cryptic exon and impaired assembly of mitochondrial complex I in a patient with Leigh syndrome Molecular Genetics and Metabolism 92 1 2 104 8 doi 10 1016 j ymgme 2007 05 010 PMID 17604671 Retrieved from https en wikipedia org w index php title NDUFS7 amp oldid 1193969580, wikipedia, wiki, book, books, library,
