NDUFS7: Difference between revisions

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{{Infobox_gene}}
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'''NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial''', also knowns as '''NADH-ubiquinone oxidoreductase 20 kDa subunit''', is an [[enzyme]] that in humans is encoded by the ''NDUFS7'' [[gene]].<ref name="pmid8938450">{{cite journal | vauthors = Hyslop SJ, Duncan AM, Pitkanen S, Robinson BH | title = Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13 | journal = Genomics | volume = 37 | issue = 3 | pages = 375–80 |date=Mar 1997 | pmid = 8938450 | pmc =  | doi = 10.1006/geno.1996.0572 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NDUFS7 NADH dehydrogenase (ubiquinone) Fe-S protein 7, 20kDa (NADH-coenzyme Q reductase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=374291| accessdate = }}</ref> The NDUFS7 protein is a subunit of [[NADH dehydrogenase (ubiquinone)]], which is located in the [[mitochondrial inner membrane]] and is the largest of the five complexes of the [[electron transport chain]].<ref name = Biochem>{{cite book|author=Donald Voet|author2=Judith G. Voet|author3=Charlotte W. Pratt|title=Fundamentals of biochemistry : life at the molecular level|date=2013|publisher=Wiley|location=Hoboken, NJ|isbn=9780470547847|chapter = 18 | pages=581–620|edition=4th}}</ref>
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==Structure==
{{GNF_Protein_box
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.<ref name="pmid22484275">{{cite journal | vauthors = Angerer H, Nasiri HR, Niedergesäß V, Kerscher S, Schwalbe H, Brandt U | title = Tracing the tail of ubiquinone in mitochondrial complex I | journal = Biochim. Biophys. Acta | volume = 1817 | issue = 10 | pages = 1776–84 |date=October 2012 | pmid = 22484275 | doi = 10.1016/j.bbabio.2012.03.021 }}</ref>
| image = 
| image_source =
| PDB =  
| Name = NADH dehydrogenase (ubiquinone) Fe-S protein 7, 20kDa (NADH-coenzyme Q reductase)
| HGNCid = 7714
| Symbol = NDUFS7
| AltSymbols =; FLJ45860; FLJ46880; MGC120002; PSST
| OMIM = 601825
| ECnumber = 
| Homologene = 11535
| MGIid = 1922656
| GeneAtlas_image1 = PBB_GE_NDUFS7_211752_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003954 |text = NADH dehydrogenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008137 |text = NADH dehydrogenase (ubiquinone) activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051539 |text = 4 iron, 4 sulfur cluster binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006120 |text = mitochondrial electron transport, NADH to ubiquinone}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 374291
    | Hs_Ensembl = ENSG00000115286
    | Hs_RefseqProtein = NP_077718
    | Hs_RefseqmRNA = NM_024407
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 1334883
    | Hs_GenLoc_end = 1346583
    | Hs_Uniprot = O75251
    | Mm_EntrezGene = 75406
    | Mm_Ensembl = ENSMUSG00000020153
    | Mm_RefseqmRNA = NM_029272
    | Mm_RefseqProtein = NP_083548
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 79652581
    | Mm_GenLoc_end = 79659921
    | Mm_Uniprot = Q9DC70
  }}
}}
'''NADH dehydrogenase (ubiquinone) Fe-S protein 7, 20kDa (NADH-coenzyme Q reductase)''', also known as '''NDUFS7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NDUFS7 NADH dehydrogenase (ubiquinone) Fe-S protein 7, 20kDa (NADH-coenzyme Q reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=374291| accessdate = }}</ref>


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==References==
{{PBB_Summary
{{reflist}}
| section_title =
| summary_text =
}}


==References==
{{reflist|2}}
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Smeitink J, van den Heuvel L |title=Human mitochondrial complex I in health and disease |journal=Am. J. Hum. Genet. |volume=64 |issue= 6 |pages= 1505–10 |year= 1999 |pmid= 10330338 |doi=10.1086/302432  | pmc=1377894 }}
| citations =
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | author=Smeitink J, van den Heuvel L |title=Human mitochondrial complex I in health and disease. |journal=Am. J. Hum. Genet. |volume=64 |issue= 6 |pages= 1505-10 |year= 1999 |pmid= 10330338 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal   |vauthors=Loeffen JL, Triepels RH, van den Heuvel LP, etal |title=cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed |journal=Biochem. Biophys. Res. Commun. |volume=253 |issue= 2 |pages= 415–22 |year= 1999 |pmid= 9878551 |doi= 10.1006/bbrc.1998.9786 }}
*{{cite journal  | author=Hyslop SJ, Duncan AM, Pitkänen S, Robinson BH |title=Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13. |journal=Genomics |volume=37 |issue= 3 |pages= 375-80 |year= 1997 |pmid= 8938450 |doi= 10.1006/geno.1996.0572 }}
*{{cite journal   |vauthors=Triepels RH, van den Heuvel LP, Loeffen JL, etal |title=Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear encoded subunit of complex I |journal=Ann. Neurol. |volume=45 |issue= 6 |pages= 787–90 |year= 1999 |pmid= 10360771 |doi=10.1002/1531-8249(199906)45:6<787::AID-ANA13>3.0.CO;2-6 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal   |vauthors=Triepels RH, Hanson BJ, van den Heuvel LP, etal |title=Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 8892–7 |year= 2001 |pmid= 11112787 |doi= 10.1074/jbc.M009903200 }}
*{{cite journal | author=Loeffen JL, Triepels RH, van den Heuvel LP, ''et al.'' |title=cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. |journal=Biochem. Biophys. Res. Commun. |volume=253 |issue= 2 |pages= 415-22 |year= 1999 |pmid= 9878551 |doi= 10.1006/bbrc.1998.9786 }}
*{{cite journal  | vauthors=Schuler F, Casida JE |title=Functional coupling of PSST and ND1 subunits in NADH:ubiquinone oxidoreductase established by photoaffinity labeling |journal=Biochim. Biophys. Acta |volume=1506 |issue= 1 |pages= 79–87 |year= 2001 |pmid= 11418099 |doi=10.1016/S0005-2728(01)00183-9 }}
*{{cite journal | author=Triepels RH, van den Heuvel LP, Loeffen JL, ''et al.'' |title=Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear encoded subunit of complex I. |journal=Ann. Neurol. |volume=45 |issue= 6 |pages= 787-90 |year= 1999 |pmid= 10360771 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Triepels RH, Hanson BJ, van den Heuvel LP, ''et al.'' |title=Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 8892-7 |year= 2001 |pmid= 11112787 |doi= 10.1074/jbc.M009903200 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Schuler F, Casida JE |title=Functional coupling of PSST and ND1 subunits in NADH:ubiquinone oxidoreductase established by photoaffinity labeling. |journal=Biochim. Biophys. Acta |volume=1506 |issue= 1 |pages= 79-87 |year= 2001 |pmid= 11418099 |doi=  }}
*{{cite journal   |vauthors=Ugalde C, Janssen RJ, van den Heuvel LP, etal |title=Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency |journal=Hum. Mol. Genet. |volume=13 |issue= 6 |pages= 659–67 |year= 2004 |pmid= 14749350 |doi= 10.1093/hmg/ddh071 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Ricci JE, Muñoz-Pinedo C, Fitzgerald P, etal |title=Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain |journal=Cell |volume=117 |issue= 6 |pages= 773–86 |year= 2004 |pmid= 15186778 |doi= 10.1016/j.cell.2004.05.008 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Lebon S, Rodriguez D, Bridoux D, etal |title=A novel mutation in the human complex I NDUFS7 subunit associated with Leigh syndrome |journal=Mol. Genet. Metab. |volume=90 |issue= 4 |pages= 379–82 |year= 2007 |pmid= 17275378 |doi= 10.1016/j.ymgme.2006.12.007 }}
*{{cite journal | author=Ugalde C, Janssen RJ, van den Heuvel LP, ''et al.'' |title=Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency. |journal=Hum. Mol. Genet. |volume=13 |issue= 6 |pages= 659-67 |year= 2004 |pmid= 14749350 |doi= 10.1093/hmg/ddh071 }}
*{{cite journal   |vauthors=Lebon S, Minai L, Chretien D, etal |title=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 |journal=Mol. Genet. Metab. |volume=92 |issue= 1–2 |pages= 104–8 |year= 2007 |pmid= 17604671 |doi= 10.1016/j.ymgme.2007.05.010 }}
*{{cite journal | author=Ricci JE, Muñoz-Pinedo C, Fitzgerald P, ''et al.'' |title=Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain. |journal=Cell |volume=117 |issue= 6 |pages= 773-86 |year= 2004 |pmid= 15186778 |doi= 10.1016/j.cell.2004.05.008 }}
*{{cite journal | author=Lebon S, Rodriguez D, Bridoux D, ''et al.'' |title=A novel mutation in the human complex I NDUFS7 subunit associated with Leigh syndrome. |journal=Mol. Genet. Metab. |volume=90 |issue= 4 |pages= 379-82 |year= 2007 |pmid= 17275378 |doi= 10.1016/j.ymgme.2006.12.007 }}
*{{cite journal | author=Lebon S, Minai L, Chretien D, ''et al.'' |title=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. |journal=Mol. Genet. Metab. |volume=92 |issue= 1-2 |pages= 104-8 |year= 2007 |pmid= 17604671 |doi= 10.1016/j.ymgme.2007.05.010 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
[[Category:Human proteins]]
{{WikiDoc Sources}}
 
 
{{gene-19-stub}}

Revision as of 12:47, 5 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial, also knowns as NADH-ubiquinone oxidoreductase 20 kDa subunit, is an enzyme that in humans is encoded by the NDUFS7 gene.[1][2] The NDUFS7 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.[3]

Structure

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.[4]

References

  1. ↑ Hyslop SJ, Duncan AM, Pitkanen S, Robinson BH (Mar 1997). "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.
  2. ↑ "Entrez Gene: NDUFS7 NADH dehydrogenase (ubiquinone) Fe-S protein 7, 20kDa (NADH-coenzyme Q reductase)".
  3. ↑ 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.
  4. ↑ Angerer H, Nasiri HR, Niedergesäß V, Kerscher S, Schwalbe H, Brandt U (October 2012). "Tracing the tail of ubiquinone in mitochondrial complex I". Biochim. Biophys. Acta. 1817 (10): 1776–84. doi:10.1016/j.bbabio.2012.03.021. PMID 22484275.

Further reading


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