Type II NAD(P)H dehydrogenases are targeted to mitochondria and chloroplasts in Arabidopsis thaliana

ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, Western Australia, Australia.
FEBS Letters (Impact Factor: 3.17). 10/2008; 582(20):3073-9. DOI: 10.1016/j.febslet.2008.07.061
Source: PubMed


We found that four type II NAD(P)H dehydrogenases (ND) in Arabidopsis are targeted to two locations in the cell; NDC1 was targeted to mitochondria and chloroplasts, while NDA1, NDA2 and NDB1 were targeted to mitochondria and peroxisomes. Targeting of NDC1 to chloroplasts as well as mitochondria was shown using in vitro and in vivo uptake assays and dual targeting of NDC1 to plastids relies on regions in the mature part of the protein. Accumulation of NDA type dehydrogenases to peroxisomes and mitochondria was confirmed using Western blot analysis on highly purified organelle fractions. Targeting of ND proteins to mitochondria and peroxisomes is achieved by two separate signals, a C-terminal signal for peroxisomes and an N-terminal signal for mitochondria.

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    • "ripening ( Nashilevitz et al . , 2010 ) , so it could play a significant bioenergetic role . However , type II NAD ( P ) H dehydrogenase may also participate in chromorespiration ( Renato et al . , 2014 ) . Type II dehydrogenases are monomeric enzymes without proton pumping activity which are targeted to mitochondria , plastids , and peroxisomes ( Carrie et al . , 2008 ) . The presence of these enzymes in chromoplasts has not been yet tested , and further studies are needed to clarify this issue . Besides , the PQ pool is also reduced by PDS , which transfers the electrons resulting from the desaturation steps of phytoene during carotenoid biosynthesis ( Norris et al . , 1995 ) ."
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    ABSTRACT: Chlororespiration is a respiratory process located in chloroplast thylakoids which consists in an electron transport chain from NAD(P)H to oxygen. This respiratory chain involves the NAD(P)H dehydrogenase complex, the plastoquinone pool and the plastid terminal oxidase (PTOX), and it probably acts as a safety valve to prevent the over-reduction of the photosynthetic machinery in stress conditions. The existence of a similar respiratory activity in non-photosynthetic plastids has been less studied. Recently, it has been reported that tomato fruit chromoplasts present an oxygen consumption activity linked to ATP synthesis. Etioplasts and amyloplasts contain several electron carriers and some subunits of the ATP synthase, so they could harbor a similar respiratory process. This review provides an update on the study about respiratory processes in chromoplasts, identifying the major gaps that need to be addressed in future research. It also reviews the proteomic data of etioplasts and amyloplasts, which suggest the presence of a respiratory electron transport chain in these plastids.
    Frontiers in Plant Science 07/2015; 6:496. DOI:10.3389/fpls.2015.00496 · 3.95 Impact Factor
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    • "ontain only traces of phylloquinone and accumulate demethyl phylloquinone rules out that other type II NADPH dehydrogenases contribute significantly to phylloquinone biosynthesis . In Arabi dopsis , such an absence of functional redundancy is not wholly unexpected because out of seven type II NADPH dehydrogenases , only NDC1 is found in plastids ( Carrie et al . , 2008 ; Xu et al . , 2013 ) . A similar scenario applies to rice , where the NDC1 ortholog is the sole plastid - targeted type II NADPH dehydrogenase ( Xu et al . , 2013 ) . By contrast , green fluorescent protein fusion experiments showed that the moss Physcomitrella patens possesses three plastid - targeted type II NADPH dehydrogenases ( Xu"
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    ABSTRACT: Mutation of Arabidopsis thaliana NAD(P)H DEHYDROGENASE C1 (NDC1; At5g08740) results in the accumulation of demethylphylloquinone, a late biosynthetic intermediate of vitamin K1. Gene coexpression and phylogenomics analyses showed that conserved functional associations occur between vitamin K biosynthesis and NDC1 homologs throughout the prokaryotic and eukaryotic lineages. Deletion of Synechocystis ndbB, which encodes for one such homolog, resulted in the same defects as those observed in the cyanobacterial demethylnaphthoquinone methyltransferase knockout. Chemical modeling and assay of purified demethylnaphthoquinone methyltransferase demonstrated that, by virtue of the strong electrophilic nature of S-adenosyl-l-methionine, the transmethylation of the demethylated precursor of vitamin K is strictly dependent on the reduced form of its naphthoquinone ring. NDC1 was shown to catalyze such a prerequisite reduction by using NADPH and demethylphylloquinone as substrates and flavine adenine dinucleotide as a cofactor. NDC1 displayed Michaelis-Menten kinetics and was markedly inhibited by dicumarol, a competitive inhibitor of naphthoquinone oxidoreductases. These data demonstrate that the reduction of the demethylnaphthoquinone ring represents an authentic step in the biosynthetic pathway of vitamin K, that this reaction is enzymatically driven, and that a selection pressure is operating to retain type II NAD(P)H dehydrogenases in this process. © 2015 American Society of Plant Biologists. All rights reserved.
    The Plant Cell 05/2015; 27(6). DOI:10.1105/tpc.15.00103 · 9.34 Impact Factor
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    • "These processes include DNA replication and repair, transcription, translation, and proteolysis. Many proteins have been found to be dual-targeted between other organelles in plants, including mitochondria, plastids and cytosol (Small et al., 1998), mitochondrion, plastid and endoplasmic reticulum (Lee et al., 2011), nucleus and cytosol (Inze et al., 2012), plastids and nucleus (Schwacke et al., 2007), mitochondria and nucleus (Krause and Krupinska, 2009), plastids and peroxisomes (Reumann et al., 2007; Sapir-Mir et al., 2008), mitochondria and peroxisomes (Carrie et al., 2008, 2009), plastid and cytosol (Kiessling et al., 2004; Thatcher et al., 2007), mitochondria and cytosol (Duchene et al., 2001), Golgi-like vesicles and cytosol (Rautengarten et al., 2011), plastids and endoplasmic reticulum (Levitan et al., 2005), and mitochondrion and endoplasmic reticulum (Lee et al., 2011). In addition, some proteins associate with the exterior of an organelle but do not penetrate the hydrophobic membrane and thus, whilst actually cytosolic, appear localized to a specific organelle (Rautengarten et al., 2011). "
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    ABSTRACT: Sub-functionalization during the expansion of gene families in eukaryotes has occurred in part through specific subcellular localization of different family members. To better understand this process in plants, compiled records of large-scale proteomic and fluorescent protein localization datasets can be explored and bioinformatic predictions for protein localization can be used to predict the gaps in experimental data. This process can be followed by targeted experiments to test predictions. The SUBA3 database is a free web-service at http://suba.plantenergy.uwa.edu.au that helps users to explore reported experimental data and predictions concerning proteins encoded by gene families and to define the experiments required to locate these homologous sets of proteins. Here we show how SUBA3 can be used to explore the subcellular location of the Deg protease family of ATP-independent serine endopeptidases (Deg1-Deg16). Combined data integration and new experiments refined location information for Deg1 and Deg9, confirmed Deg2, Deg5, and Deg8 in plastids and Deg 15 in peroxisomes and provide substantial experimental evidence for mitochondrial localized Deg proteases. Two of these, Deg3 and Deg10, additionally localized to the plastid, revealing novel dual-targeted Deg proteases in the plastid and the mitochondrion. SUBA3 is continually updated to ensure that researchers can use the latest published data when planning the experimental steps remaining to localize gene family functions.
    Frontiers in Plant Science 08/2014; 5:396. DOI:10.3389/fpls.2014.00396 · 3.95 Impact Factor
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