L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana

L-Galactono-1,4-lactone dehydrogenase (GLDH) catalyzes the terminal step of the Smirnoff-Wheeler pathway for vitamin C (L-ascorbate) biosynthesis in plants. A GLDH in gel activity assay was developed to biochemically investigate GLDH localization in plant mitochondria. It previously has been shown t...

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Autores principales: Schertl, Peter, Sunderhaus, Stephanie, Klodmann, Jennifer, Gergoff Grozeff, Gustavo Esteban, Bartoli, Carlos Guillermo, Braun, Hans Peter
Formato: Articulo
Lenguaje:Inglés
Publicado: 2012
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/84999
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id I19-R120-10915-84999
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Plantas
Arabidopsis
spellingShingle Biología
Plantas
Arabidopsis
Schertl, Peter
Sunderhaus, Stephanie
Klodmann, Jennifer
Gergoff Grozeff, Gustavo Esteban
Bartoli, Carlos Guillermo
Braun, Hans Peter
L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana
topic_facet Biología
Plantas
Arabidopsis
description L-Galactono-1,4-lactone dehydrogenase (GLDH) catalyzes the terminal step of the Smirnoff-Wheeler pathway for vitamin C (L-ascorbate) biosynthesis in plants. A GLDH in gel activity assay was developed to biochemically investigate GLDH localization in plant mitochondria. It previously has been shown that GLDH forms part of an 850-kDa complex that represents a minor form of the respiratory NADH dehydrogenase complex (complex I). Because accumulation of complex I is disturbed in the absence of GLDH, a role of this enzyme in complex I assembly has been proposed. Here we report that GLDH is associated with two further protein complexes. Using native gel electrophoresis procedures in combination with the in gel GLDH activity assay and immunoblotting, two mitochondrial complexes of 470 and 420 kDa were identified. Both complexes are of very low abundance. Protein identifications by mass spectrometry revealed that they include subunits of complex I. Finally, the 850-kDa complex was further investigated and shown to include the complete "peripheral arm" of complex I. GLDH is attached to a membrane domain, which represents a major fragment of the "membrane arm" of complex I. Taken together, our data further support a role of GLDH during complex I formation, which is based on its binding to specific assembly intermediates.
format Articulo
Articulo
author Schertl, Peter
Sunderhaus, Stephanie
Klodmann, Jennifer
Gergoff Grozeff, Gustavo Esteban
Bartoli, Carlos Guillermo
Braun, Hans Peter
author_facet Schertl, Peter
Sunderhaus, Stephanie
Klodmann, Jennifer
Gergoff Grozeff, Gustavo Esteban
Bartoli, Carlos Guillermo
Braun, Hans Peter
author_sort Schertl, Peter
title L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana
title_short L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana
title_full L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana
title_fullStr L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana
title_full_unstemmed L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana
title_sort l-galactono-1,4-lactone dehydrogenase (gldh) forms part of three subcomplexes of mitochondrial complex i in arabidopsis thaliana
publishDate 2012
url http://sedici.unlp.edu.ar/handle/10915/84999
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