scholarly journals Molecular identification of three Arabidopsis thaliana mitochondrial dicarboxylate carrier isoforms: organ distribution, bacterial expression, reconstitution into liposomes and functional characterization

2008 ◽  
Vol 410 (3) ◽  
pp. 621-629 ◽  
Author(s):  
Luigi Palmieri ◽  
Nathalie Picault ◽  
Roberto Arrigoni ◽  
Evelyne Besin ◽  
Ferdinando Palmieri ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Functional Characterization ◽  
Dicarboxylic Acids ◽  
Uncoupling Proteins ◽  
Organ Distribution ◽  
Mitochondrial Carrier ◽  
Wide Range ◽  
Mitochondrial Carrier Family ◽  
Arabidopsis Thaliana Genome

Screening of the Arabidopsis thaliana genome revealed three potential homologues of mammalian and yeast mitochondrial DICs (dicarboxylate carriers) designated as DIC1, DIC2 and DIC3, each belonging to the mitochondrial carrier protein family. DIC1 and DIC2 are broadly expressed at comparable levels in all the tissues investigated. DIC1–DIC3 have been reported previously as uncoupling proteins, but direct transport assays with recombinant and reconstituted DIC proteins clearly demonstrate that their substrate specificity is unique to plants, showing the combined characteristics of the DIC and oxaloacetate carrier in yeast. Indeed, the Arabidopsis DICs transported a wide range of dicarboxylic acids including malate, oxaloacetate and succinate as well as phosphate, sulfate and thiosulfate at high rates, whereas 2-oxoglutarate was revealed to be a very poor substrate. The role of these plant mitochondrial DICs is discussed with respect to other known mitochondrial carrier family members including uncoupling proteins. It is proposed that plant DICs constitute the membrane component of several metabolic processes including the malate–oxaloacetate shuttle, the most important redox connection between the mitochondria and the cytosol.

Computational studies of the mitochondrial carrier family SLC25. Present status and future perspectives

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Andrea Pasquadibisceglie ◽  
Fabio Polticelli
Keyword(s):  
Transport Mechanism ◽  
Experimental Studies ◽  
Intermembrane Space ◽  
Mitochondrial Carrier ◽  
Mitochondrial Homeostasis ◽  
The Matrix ◽  
Mitochondrial Carrier Family ◽  
Mitochondrial Intermembrane Space ◽  
Computational Analyses

Abstract The members of the mitochondrial carrier family, also known as solute carrier family 25 (SLC25), are transmembrane proteins involved in the translocation of a plethora of small molecules between the mitochondrial intermembrane space and the matrix. These transporters are characterized by three homologous domains structure and a transport mechanism that involves the transition between different conformations. Mutations in regions critical for these transporters’ function often cause several diseases, given the crucial role of these proteins in the mitochondrial homeostasis. Experimental studies can be problematic in the case of membrane proteins, in particular concerning the characterization of the structure–function relationships. For this reason, computational methods are often applied in order to develop new hypotheses or to support/explain experimental evidence. Here the computational analyses carried out on the SLC25 members are reviewed, describing the main techniques used and the outcome in terms of improved knowledge of the transport mechanism. Potential future applications on this protein family of more recent and advanced in silico methods are also suggested.

scholarly journals Functional characterization and organ distribution of three mitochondrial ATP–Mg/Pi carriers in Arabidopsis thaliana

2015 ◽  
Vol 1847 (10) ◽  
pp. 1220-1230 ◽  
Author(s):  
Magnus Monné ◽  
Daniela Valeria Miniero ◽  
Toshihiro Obata ◽  
Lucia Daddabbo ◽  
Luigi Palmieri ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Functional Characterization ◽  
Organ Distribution

scholarly journals Uncoupling proteins in mitochondria of plants and some microorganisms.

2001 ◽  
Vol 48 (1) ◽  
pp. 145-155 ◽  
Author(s):  
W Jarmuszkiewicz
Keyword(s):  
Higher Plants ◽  
Uncoupling Protein ◽  
Physiological Role ◽  
Acanthamoeba Castellanii ◽  
Uncoupling Proteins ◽  
Protein Activity ◽  
Functional Connection ◽  
Mitochondrial Inner Membrane ◽  
Mitochondrial Carrier Family

Uncoupling proteins, members of the mitochondrial carrier family, are present in mitochondrial inner membrane and mediate free fatty acid-activated, purine-nucleotide-inhibited H+ re-uptake. Since 1995, it has been shown that the uncoupling protein is present in many higher plants and some microorganisms like non-photosynthetic amoeboid protozoon, Acanthamoeba castellanii and non-fermentative yeast Candida parapsilosis. In mitochondria of these organisms, uncoupling protein activity is revealed not only by stimulation of state 4 respiration by free fatty acids accompanied by decrease in membrane potential (these effects being partially released by ATP and GTP) but mainly by lowering ADP/O ratio during state 3 respiration. Plant and microorganism uncoupling proteins are able to divert very efficiently energy from oxidative phosphorylation, competing for deltamicroH+ with ATP synthase. Functional connection and physiological role of uncoupling protein and alternative oxidase, two main energy-dissipating systems in plant-type mitochondria, are discussed.

scholarly journals Characterization of In Vivo Function(s) of Members of the Plant Mitochondrial Carrier Family

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1226
Author(s):  
Adriano Nunes-Nesi ◽  
João Henrique F. Cavalcanti ◽  
Alisdair R. Fernie
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Genetic Variants ◽  
Mitochondrial Carrier ◽  
Wide Range ◽  
Mitochondrial Carrier Family ◽  
Insight Into ◽  
Green Lineage

Although structurally related, mitochondrial carrier family (MCF) proteins catalyze the specific transport of a range of diverse substrates including nucleotides, amino acids, dicarboxylates, tricarboxylates, cofactors, vitamins, phosphate and H+. Despite their name, they do not, however, always localize to the mitochondria, with plasma membrane, peroxisomal, chloroplast and thylakoid and endoplasmic reticulum localizations also being reported. The existence of plastid-specific MCF proteins is suggestive that the evolution of these proteins occurred after the separation of the green lineage. That said, plant-specific MCF proteins are not all plastid-localized, with members also situated at the endoplasmic reticulum and plasma membrane. While by no means yet comprehensive, the in vivo function of a wide range of these transporters is carried out here, and we discuss the employment of genetic variants of the MCF as a means to provide insight into their in vivo function complementary to that obtained from studies following their reconstitution into liposomes.

scholarly journals Structural and functional characterization of human and murine C5a anaphylatoxins

2014 ◽  
Vol 70 (6) ◽  
pp. 1704-1717 ◽  
Author(s):  
Janus Asbjørn Schatz-Jakobsen ◽  
Laure Yatime ◽  
Casper Larsen ◽  
Steen Vang Petersen ◽  
Andreas Klos ◽  
...  
Keyword(s):  
Complement Activation ◽  
Functional Characterization ◽  
Functional Assay ◽  
Helix Bundle ◽  
Wide Range ◽  
A Cell ◽  
Four Helix Bundle ◽  
G Protein Coupled

Complement is an ancient part of the innate immune system that plays a pivotal role in protection against invading pathogens and helps to clear apoptotic and necrotic cells. Upon complement activation, a cascade of proteolytic events generates the complement effectors, including the anaphylatoxins C3a and C5a. Signalling through their cognate G-protein coupled receptors, C3aR and C5aR, leads to a wide range of biological events promoting inflammation at the site of complement activation. The function of anaphylatoxins is regulated by circulating carboxypeptidases that remove their C-terminal arginine residue, yielding C3a-desArg and C5a-desArg. Whereas human C3a and C3a-desArg adopt a canonical four-helix bundle fold, the conformation of human C5a-desArg has recently been described as a three-helix bundle. Here, the crystal structures of an antagonist version of human C5a, A8Δ71–73, and of murine C5a and C5a-desArg are reported. Whereas A8Δ71–73adopts a three-helix bundle conformation similar to human C5a-desArg, the two murine proteins form a four-helix bundle. A cell-based functional assay reveals that murine C5a-desArg, in contrast to its human counterpart, exerts the same level of activition as murine C5a on its cognate receptor. The role of the different C5a conformations is discussed in relation to the differential activation of C5a receptors across species.

scholarly journals Peroxisomal Cofactor Transport

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1174
Author(s):  
Anastasija Plett ◽  
Lennart Charton ◽  
Nicole Linka
Keyword(s):  
Endoplasmic Reticulum ◽  
Nicotinamide Adenine Dinucleotide ◽  
Metabolic Pathways ◽  
Growth And Development ◽  
Current Knowledge ◽  
Peroxisomal Membrane ◽  
Mitochondrial Carrier ◽  
Wide Range ◽  
Mitochondrial Carrier Family ◽  
Cellular Organelles

Peroxisomes are eukaryotic organelles that are essential for growth and development. They are highly metabolically active and house many biochemical reactions, including lipid metabolism and synthesis of signaling molecules. Most of these metabolic pathways are shared with other compartments, such as Endoplasmic reticulum (ER), mitochondria, and plastids. Peroxisomes, in common with all other cellular organelles are dependent on a wide range of cofactors, such as adenosine 5′-triphosphate (ATP), Coenzyme A (CoA), and nicotinamide adenine dinucleotide (NAD). The availability of the peroxisomal cofactor pool controls peroxisome function. The levels of these cofactors available for peroxisomal metabolism is determined by the balance between synthesis, import, export, binding, and degradation. Since the final steps of cofactor synthesis are thought to be located in the cytosol, cofactors must be imported into peroxisomes. This review gives an overview about our current knowledge of the permeability of the peroxisomal membrane with the focus on ATP, CoA, and NAD. Several members of the mitochondrial carrier family are located in peroxisomes, catalyzing the transfer of these organic cofactors across the peroxisomal membrane. Most of the functions of these peroxisomal cofactor transporters are known from studies in yeast, humans, and plants. Parallels and differences between the transporters in the different organisms are discussed here.

scholarly journals Overexpression of ANAC046 Promotes Suberin Biosynthesis in Roots of Arabidopsis thaliana

2019 ◽  
Vol 20 (24) ◽  
pp. 6117 ◽  
Author(s):  
Kashif Mahmood ◽  
Viktoria Valeska Zeisler-Diehl ◽  
Lukas Schreiber ◽  
Yong-Mei Bi ◽  
Steven J. Rothstein ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Pcr Analysis ◽  
Transcription Activator ◽  
Cuticular Waxes ◽  
Plant Parts ◽  
Wide Range ◽  
Transgenic Lines ◽  
Blue Stain ◽  
Root Endodermis

NAC (NAM (no apical meristem), ATAF1/2, and CUC2 (cup-shaped cotyledon)) proteins are one of the largest families of plant-specific transcription factors, and this family is present in a wide range of land plants. Here, we have investigated the role of ANAC046 in the regulation of suberin biosynthesis and deposition in Arabidopsis. Subcellular localization and transcriptional activity assays showed that ANAC046 localizes in the nucleus, where it functions as a transcription activator. Analysis of the PANAC046:GUS lines revealed that ANAC046 is mainly expressed in the root endodermis and periderm, and is also induced in leaves by wounding. The transgenic lines overexpressing ANAC046 exhibited defective surfaces on the aerial plant parts compared to the wild-type (WT) as characterized by increased permeability for Toluidine blue stain and greater chlorophyll leaching. Quantitative RT-PCR analysis showed that the expression of suberin biosynthesis genes was significantly higher in the roots and leaves of overexpression lines compared to the WT. The biochemical analysis of leaf cuticular waxes showed that the overexpression lines accumulated 30% more waxes than the WT. Concurrently, overexpression lines also deposited almost twice the amount of suberin content in their roots compared with the WT. Taken together, these results showed that ANAC046 is an important transcription factor that promotes suberin biosynthesis in Arabidopsis thaliana roots.

Uncoupling Proteins: Do They Have a Role in Body Weight Regulation?

Physiology ◽  
2000 ◽  
Vol 15 (6) ◽  
pp. 313-318 ◽  
Author(s):  
Abdul.G. Dulloo ◽  
Sonia Samec
Keyword(s):  
Uncoupling Protein ◽  
Physiological Role ◽  
Uncoupling Proteins ◽  
Weight Regulation ◽  
Body Weight Regulation ◽  
Mitochondrial Carrier ◽  
Adaptive Thermogenesis ◽  
Brown Adipose ◽  
Mitochondrial Carrier Protein

Several members of the mitochondrial carrier protein family are classified as uncoupling proteins. In contrast to the uncoupling protein specific to brown adipose tissue (UCP1), the physiological role of skeletal muscle uncoupling proteins (UCP2 and UCP3) in weight regulation seems more closely associated with the regulation of lipids as fuel substrate than as mediators of adaptive thermogenesis.

The Problem of Identifying and Modeling the Relationship between Monetary Factor and Inflation in the Russian Economy

2008 ◽  
pp. 61-76
Author(s):  
A. Porshakov ◽  
A. Ponomarenko
Keyword(s):  
Money Supply ◽  
Money Demand ◽  
Russian Economy ◽  
Long Run ◽  
Complex Approach ◽  
Wide Range ◽  
Long Time ◽  
The Relationship ◽  
Supply Side Factors

The role of monetary factor in generating inflationary processes in Russia has stimulated various debates in social and scientific circles for a relatively long time. The authors show that identification of the specificity of relationship between money and inflation requires a complex approach based on statistical modeling and involving a wide range of indicators relevant for the price changes in the economy. As a result a model of inflation for Russia implying the decomposition of inflation dynamics into demand-side and supply-side factors is suggested. The main conclusion drawn is that during the recent years the volume of inflationary pressures in the Russian economy has been determined by the deviation of money supply from money demand, rather than by money supply alone. At the same time, monetary factor has a long-run spread over time impact on inflation.

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