English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/155054
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 12 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2)

Autor Sato, Motoaki; Sinha, Prem Kumar; Torres-Bacete, Jesús; Matsuno-Yagi, Akemi; Yagi, Takao
Palabras clave Bioenergetics
Electron Transport System (ETS)
Membrane Energetics
Membrane Enzymes
NADH Dehydrogenase
Site-directed Mutagenesis
Fecha de publicación 23-ago-2013
EditorAmerican Society for Biochemistry and Molecular Biology
Citación J Biol Chem. 288(34):24705-16 (2013)
ResumenThe proton-translocating NADH-quinone oxidoreductase (complex I/NDH-1) contains a peripheral and a membrane domain. Three antiporter-like subunits in the membrane domain, NuoL, NuoM, and NuoN (ND5, ND4 and ND2, respectively), are structurally similar. We analyzed the role of NuoN in Escherichia coli NDH-1. The lysine residue at position 395 in NuoN (NLys(395)) is conserved in NuoL (LLys(399)) but is replaced by glutamic acid (MGlu(407)) in NuoM. Our mutation study on NLys(395) suggests that this residue participates in the proton translocation. Furthermore, we found that MGlu(407) is also essential and most likely interacts with conserved LArg(175). Glutamic acids, NGlu(133), MGlu(144), and LGlu(144), are corresponding residues. Unlike mutants of MGlu(144) and LGlu(144), mutation of NGlu(133) scarcely affected the energy-transducing activities. However, a double mutant of NGlu(133) and nearby KGlu(72) showed significant inhibition of these activities. This suggests that NGlu(133) bears a functional role similar to LGlu(144) and MGlu(144) but its mutation can be partially compensated by the nearby carboxyl residue. Conserved prolines located at loops of discontinuous transmembrane helices of NuoL, NuoM, and NuoN were shown to play a similar role in the energy-transducing activity. It seems likely that NuoL, NuoM, and NuoN pump protons by a similar mechanism. Our data also revealed that NLys(158) is one of the key interaction points with helix HL in NuoL. A truncation study indicated that the C-terminal amphipathic segments of NTM14 interacts with the Mβ sheet located on the opposite side of helix HL. Taken together, the mechanism of H(+) translocation in NDH-1 is discussed.
Descripción 13 p.-7 fig.-3 tab.
Versión del editorhttp://dx.doi.org/ 10.1074/jbc.M113.482968
URI http://hdl.handle.net/10261/155054
DOI10.1074/jbc.M113.482968
ISSN0021-9258
E-ISSN1083-351X
Aparece en las colecciones: (CIB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
J. Biol. Chem.-2013-Sato-24705-16.pdfArtículo principal3,1 MBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.