Difference between revisions of "Angerer 2014 Proc Natl Acad Sci U S A"
(Created page with "{{Publication |title=Angerer H, Radermacher M, Mańkowska M, Steger M, Zwicker K, Heide H, Wittig I, Brandt U, Zickermann V (2014) The LYR protein subunit NB4M/NDUFA6 of mitoc...") |
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|title=Angerer H, Radermacher M, Mańkowska M, Steger M, Zwicker K, Heide H, Wittig I, Brandt U, Zickermann V (2014) The LYR protein subunit NB4M/NDUFA6 of mitochondrial complex I anchors an acyl carrier protein and is essential for catalytic activity. https://doi.org/10.1073/pnas.1322438111 | |title=Angerer H, Radermacher M, Mańkowska M, Steger M, Zwicker K, Heide H, Wittig I, Brandt U, Zickermann V (2014) The LYR protein subunit NB4M/NDUFA6 of mitochondrial complex I anchors an acyl carrier protein and is essential for catalytic activity. https://doi.org/10.1073/pnas.1322438111 | ||
|info=Proc Natl Acad Sci U S A 111:5207-12. [https://www.ncbi.nlm.nih.gov/pubmed/24706851 PMID: 24706851 Open Access] | |info=Proc Natl Acad Sci U S A 111:5207-12. [https://www.ncbi.nlm.nih.gov/pubmed/24706851 PMID: 24706851 Open Access] | ||
|authors=Angerer | |authors=Angerer Heike, Radermacher Michael, Mankowska Michalina, Steger Micro, Zwicker Klaus, Heide Heinrich, Wittig Ilka, Brandt Ulrich, Zickermann Volker | ||
|year=2014 | |year=2014 | ||
|journal=Proc Natl Acad Sci U S A | |journal=Proc Natl Acad Sci U S A | ||
|abstract=Mitochondrial complex I is the largest and most complicated enzyme of the oxidative phosphorylation system. It comprises a number of so-called accessory subunits of largely unknown structure and function. Here we studied subunit NB4M [NDUFA6, LYR motif containing protein 6 (LYRM6)], a member of the LYRM family of proteins. Chromosomal deletion of the corresponding gene in the yeast Yarrowia lipolytica caused concomitant loss of the mitochondrial acyl carrier protein subunit ACPM1 from the enzyme complex and paralyzed ubiquinone reductase activity. Exchanging the LYR motif and an associated conserved phenylalanine by alanines in subunit NB4M also abolished the activity and binding of subunit ACPM1. We show, by single-particle electron microscopy and structural modeling, that subunits NB4M and ACPM1 form a subdomain that protrudes from the peripheral arm in the vicinity of central subunit domains known to be involved in controlling the catalytic activity of complex I. | |abstract=Mitochondrial complex I is the largest and most complicated enzyme of the oxidative phosphorylation system. It comprises a number of so-called accessory subunits of largely unknown structure and function. Here we studied subunit NB4M [NDUFA6, LYR motif containing protein 6 (LYRM6)], a member of the LYRM family of proteins. Chromosomal deletion of the corresponding gene in the yeast ''Yarrowia lipolytica'' caused concomitant loss of the mitochondrial acyl carrier protein subunit ACPM1 from the enzyme complex and paralyzed ubiquinone reductase activity. Exchanging the LYR motif and an associated conserved phenylalanine by alanines in subunit NB4M also abolished the activity and binding of subunit ACPM1. We show, by single-particle electron microscopy and structural modeling, that subunits NB4M and ACPM1 form a subdomain that protrudes from the peripheral arm in the vicinity of central subunit domains known to be involved in controlling the catalytic activity of complex I. | ||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
}} | }} | ||
{{Labeling}} | {{Labeling | ||
|area=mt-Structure;fission;fusion | |||
|enzymes=Complex I | |||
}} | |||
Latest revision as of 15:31, 28 March 2023
| Angerer H, Radermacher M, Mańkowska M, Steger M, Zwicker K, Heide H, Wittig I, Brandt U, Zickermann V (2014) The LYR protein subunit NB4M/NDUFA6 of mitochondrial complex I anchors an acyl carrier protein and is essential for catalytic activity. https://doi.org/10.1073/pnas.1322438111 |
» Proc Natl Acad Sci U S A 111:5207-12. PMID: 24706851 Open Access
Angerer Heike, Radermacher Michael, Mankowska Michalina, Steger Micro, Zwicker Klaus, Heide Heinrich, Wittig Ilka, Brandt Ulrich, Zickermann Volker (2014) Proc Natl Acad Sci U S A
Abstract: Mitochondrial complex I is the largest and most complicated enzyme of the oxidative phosphorylation system. It comprises a number of so-called accessory subunits of largely unknown structure and function. Here we studied subunit NB4M [NDUFA6, LYR motif containing protein 6 (LYRM6)], a member of the LYRM family of proteins. Chromosomal deletion of the corresponding gene in the yeast Yarrowia lipolytica caused concomitant loss of the mitochondrial acyl carrier protein subunit ACPM1 from the enzyme complex and paralyzed ubiquinone reductase activity. Exchanging the LYR motif and an associated conserved phenylalanine by alanines in subunit NB4M also abolished the activity and binding of subunit ACPM1. We show, by single-particle electron microscopy and structural modeling, that subunits NB4M and ACPM1 form a subdomain that protrudes from the peripheral arm in the vicinity of central subunit domains known to be involved in controlling the catalytic activity of complex I.
• Bioblast editor: Plangger M
Labels: MiParea: mt-Structure;fission;fusion
Enzyme: Complex I
