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  1. Article: Functional characterization and purification of a Saccharomyces cerevisiae ADP/ATP carrier-iso 1 cytochrome c fusion protein.

    Dassa, Emmanuel Philippe / Dahout-Gonzalez, Cécile / Dianoux, Anne-Christine / Brandolin, Gérard

    Protein expression and purification

    2005  Volume 40, Issue 2, Page(s) 358–369

    Abstract: ... cytochrome c (Cyc1p), both from Saccharomyces cerevisiae, has been genetically elaborated with the aim ...

    Abstract A recombinant fusion protein combining the mitochondrial ADP/ATP carrier (Anc2p) and the iso-1-cytochrome c (Cyc1p), both from Saccharomyces cerevisiae, has been genetically elaborated with the aim of increasing the polar surface area of the carrier to facilitate its crystallization. The gene encoding the his-tagged fusion protein was expressed in yeast under the control of the regulatory sequences of ScANC2. The chimeric carrier, Anc2-Cyc1(His6)p, was able to restore growth on a non-fermentable carbon source of a yeast strain devoid of functional ADP/ATP carrier, which demonstrated its transport activity. The kinetic exchange properties of Anc2-Cyc1(His6)p and the wild type his-tagged carrier Anc2(His6)p were very similar. However, Anc2-Cyc1(His6)p restored cell growth less efficiently than Anc2(His6)p which correlates with the lower amount found in mitochondria. Purification of Anc2-Cyc1(His6)p in complex with carboxyatractyloside (CATR), a high affinity inhibitor of ADP/ATP transport, was achieved by combining ion-exchange chromatography and ion-metal affinity chromatography in the presence of LAPAO, an aminoxide detergent. As characterized by absorption in the visible range, heme was found to be present in isolated Anc2-Cyc1(His6)p, giving the protein a red color. Large-scale purification of Anc2-Cyc1(His6)p-CATR complex opens up novel possibilities for the use of crystallographic approaches to the yeast ADP/ATP carrier.
    MeSH term(s) Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Atractyloside/analogs & derivatives ; Chromatography/methods ; Cloning, Molecular/methods ; Crystallization ; Cytochromes c/genetics ; Cytochromes c/isolation & purification ; Escherichia coli/genetics ; Genetic Engineering ; Heme ; Histidine ; Kinetics ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/isolation & purification ; Mitochondrial ADP, ATP Translocases/metabolism ; Molecular Probes ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/isolation & purification ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/isolation & purification ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances CYC1 protein, S cerevisiae ; Molecular Probes ; PET9 protein, S cerevisiae ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins ; Atractyloside (17754-44-8) ; Heme (42VZT0U6YR) ; Histidine (4QD397987E) ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Cytochromes c (9007-43-6) ; Mitochondrial ADP, ATP Translocases (9068-80-8) ; carboxyatractyloside (SNP1XL23E6)
    Language English
    Publishing date 2005-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1055455-5
    ISSN 1096-0279 ; 1046-5928
    ISSN (online) 1096-0279
    ISSN 1046-5928
    DOI 10.1016/j.pep.2004.12.019
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  2. Article ; Online: Native membrane proteins vs. yeast recombinant: an example: the mitochondrial ADP/ATP carrier.

    Arnou, Bertrand / Dahout-Gonzalez, Cécile / Pelosi, Ludovic / Lauquin, Guy J-M / Brandolin, Gérard / Trézéguet, Véronique

    Methods in molecular biology (Clifton, N.J.)

    2010  Volume 654, Page(s) 19–28

    Abstract: ... the purification yield and quality of the chimera tagged either with six histidines at its C-ter end or nine ...

    Abstract The mitochondrial ADP/ATP carrier (Ancp) has long been a paradigm for studies of the mitochondrial carrier family due to, among other properties, its natural abundance and the existence of specific inhibitors, namely, carboxyatractyloside (CATR) and bongkrekic acid (BA), which lock the carrier under distinct and stable conformations. Bovine Anc1p isolated in complex with CATR in the presence of an aminoxyde detergent (LAPAO) was crystallized and its 3D structure determined. It is the first mitochondrial carrier structure resolved at high resolution (2.2 A, as reported by Pebay-Peyroula et al. (Nature 426:39-44, 2003)). Analyses revealed a monomer while most of the biochemical studies led to hypothesize Ancp functions as a dimer. To address the structural organization issue, we engineered a mutant of the yeast Ancp that corresponds to a covalent homodimer in view of 3D structure determination. We compare in this chapter the purification yield and quality of the chimera tagged either with six histidines at its C-ter end or nine histidines at its N-ter. We show that, as expected, length and position of the tag are important criteria for qualitative purification. We also discuss the advantages and drawbacks of purifying Ancp either from a natural source or from engineered yeast cells.
    MeSH term(s) Animals ; Atractyloside/analogs & derivatives ; Atractyloside/chemistry ; Atractyloside/pharmacology ; Bongkrekic Acid/chemistry ; Bongkrekic Acid/pharmacology ; Cattle ; Membrane Proteins/antagonists & inhibitors ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondrial ADP, ATP Translocases/antagonists & inhibitors ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/metabolism ; Recombinant Proteins/antagonists & inhibitors ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
    Chemical Substances Membrane Proteins ; Recombinant Proteins ; Bongkrekic Acid (11076-19-0) ; Atractyloside (17754-44-8) ; Mitochondrial ADP, ATP Translocases (9068-80-8) ; carboxyatractyloside (SNP1XL23E6)
    Language English
    Publishing date 2010
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-60761-762-4_2
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  3. Article: Crystallization of the bovine ADP/ATP carrier is critically dependent upon the detergent-to-protein ratio.

    Dahout-Gonzalez, Cécile / Brandolin, Gérard / Pebay-Peyroula, Eva

    Acta crystallographica. Section D, Biological crystallography

    2003  Volume 59, Issue Pt 12, Page(s) 2353–2355

    Abstract: The ADP/ATP carrier is an integral membrane protein located in the mitochondrial inner membrane. It mediates the exchange of cytosolic ADP for ATP generated in the mitochondrial matrix. Here, the purification and crystallization of the bovine ADP/ATP ... ...

    Abstract The ADP/ATP carrier is an integral membrane protein located in the mitochondrial inner membrane. It mediates the exchange of cytosolic ADP for ATP generated in the mitochondrial matrix. Here, the purification and crystallization of the bovine ADP/ATP carrier in complex with the inhibitor carboxyatractyloside in the presence of LAPAO, an aminoxide detergent, is reported. High-quality crystals were only obtained when excess detergent was removed to reach a controlled detergent-to-protein ratio.
    MeSH term(s) Animals ; Cattle ; Crystallization ; Crystallography, X-Ray ; Detergents/chemistry ; Laurates/chemistry ; Mitochondrial ADP, ATP Translocases/chemistry ; Models, Molecular
    Chemical Substances Detergents ; Laurates ; LAPAO (61792-31-2) ; Mitochondrial ADP, ATP Translocases (9068-80-8)
    Language English
    Publishing date 2003-11-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2968623-4
    ISSN 2059-7983 ; 0907-4449
    ISSN (online) 2059-7983
    ISSN 0907-4449
    DOI 10.1107/s0907444903020699
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  4. Article ; Online: PBP active site flexibility as the key mechanism for beta-lactam resistance in pneumococci.

    Contreras-Martel, Carlos / Dahout-Gonzalez, Cécile / Martins, Alexandre Dos Santos / Kotnik, Miha / Dessen, Andréa

    Journal of molecular biology

    2009  Volume 387, Issue 4, Page(s) 899–909

    Abstract: Penicillin-binding proteins (PBPs), the main targets of beta-lactam antibiotics, are membrane-associated enzymes that catalyze the two last steps in the biosynthesis of peptidoglycan. In Streptococcus pneumoniae, a major human pathogen, the surge in ... ...

    Abstract Penicillin-binding proteins (PBPs), the main targets of beta-lactam antibiotics, are membrane-associated enzymes that catalyze the two last steps in the biosynthesis of peptidoglycan. In Streptococcus pneumoniae, a major human pathogen, the surge in resistance to such antibiotics is a direct consequence of the proliferation of mosaic PBP-encoding genes, which give rise to proteins containing tens of mutations. PBP2b is a major drug resistance target, and its modification is essential for the development of high levels of resistance to piperacillin. In this work, we have solved the crystal structures of PBP2b from a wild-type pneumococcal strain, as well as from a highly drug-resistant clinical isolate displaying 58 mutations. Although mutations are present throughout the entire PBP structure, those surrounding the active site influence the total charge and the polar character of the region, while those in close proximity to the catalytic nucleophile impart flexibility onto the beta3/beta4 loop area, which encapsulates the cleft. The wealth of structural data on pneumococcal PBPs now underlines the importance of high malleability in active site regions of drug-resistant strains, suggesting that active site "breathing" could be a common mechanism employed by this pathogen to prevent targeting by beta-lactams.
    MeSH term(s) Amino Acid Sequence ; Binding Sites/genetics ; Crystallography, X-Ray ; Genes, Bacterial ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Penicillin-Binding Proteins/chemistry ; Penicillin-Binding Proteins/genetics ; Penicillin-Binding Proteins/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Streptococcus pneumoniae/drug effects ; Streptococcus pneumoniae/genetics ; Streptococcus pneumoniae/metabolism ; Streptococcus pneumoniae/pathogenicity ; beta-Lactam Resistance/genetics ; beta-Lactam Resistance/physiology
    Chemical Substances Penicillin-Binding Proteins
    Language English
    Publishing date 2009-04-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2009.02.024
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  5. Article: Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers.

    Nury, H / Dahout-Gonzalez, C / Trézéguet, V / Lauquin, G / Brandolin, G / Pebay-Peyroula, E

    FEBS letters

    2005  Volume 579, Issue 27, Page(s) 6031–6036

    Abstract: The oligomerization state of the ADP/ATP carrier is an important issue in understanding the mechanism underlying nucleotide exchange across the inner mitochondrial membrane. The first high resolution structure obtained in the presence of ... ...

    Abstract The oligomerization state of the ADP/ATP carrier is an important issue in understanding the mechanism underlying nucleotide exchange across the inner mitochondrial membrane. The first high resolution structure obtained in the presence of carboxyatractyloside revealed a large cavity formed within a monomer in which the inhibitor is strongly bound. Whereas the protein-protein interactions implicated in the first crystal form are not biologically relevant, the new crystal form described herein, highlights favorable protein-protein interactions. The interactions are mediated by endogenous cardiolipins, which are tightly bound to the protein, two cardiolipins being sandwiched between the monomers on the matrix side. The putative dimerization interface evidenced here is consistent with other structural, biochemical or functional data published so far.
    MeSH term(s) Animals ; Cardiolipins/chemistry ; Cattle ; Crystallography, X-Ray ; Mitochondrial ADP, ATP Translocases/chemistry ; Protein Conformation ; Protein Interaction Mapping
    Chemical Substances Cardiolipins ; Mitochondrial ADP, ATP Translocases (9068-80-8)
    Language English
    Publishing date 2005-11-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2005.09.061
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  6. Article: Conformation-dependent swinging of the matrix loop m2 of the mitochondrial Saccharomyces cerevisiae ADP/ATP carrier.

    Dahout-Gonzalez, Cécile / Ramus, Claire / Dassa, Emmanuel Philippe / Dianoux, Anne-Christine / Brandolin, Gérard

    Biochemistry

    2005  Volume 44, Issue 49, Page(s) 16310–16320

    Abstract: ... involved in the translocation process. The proteolysis approach allowed us to demonstrate (i) that N- and C ...

    Abstract Structure-function relationships of the membrane-embedded Saccharomyces cerevisiae mitochondrial ADP/ATP carrier were investigated through two independent approaches, namely, limited proteolysis and cysteine labeling. Experiments were carried out in the presence of either carboxyatractyloside (CATR) or bongkrekic acid (BA), two specific inhibitors of the ADP/ATP transport that bind to two distinct conformers involved in the translocation process. The proteolysis approach allowed us to demonstrate (i) that N- and C-terminal extremities of ADP/ATP carrier are facing the intermembrane space and (ii) that the central region of the carrier corresponding to the matrix loop m2 is accessible to externally added trypsin in a conformation-sensitive manner, being cleaved at the Lys163-Gly164 and Lys178-Thr179 bonds in the carrier-CATR and the carrier-BA complexes, respectively. The cysteine labeling approach was carried out on the S161C mutant of the ADP/ATP carrier. This variant of the carrier is fully active, displaying nucleotide transport kinetic parameters and inhibitor binding properties similar to that of wild-type carrier. Alkylation experiments, carried out on mitochondria with the nonpermeable reagents eosin-5-maleimide and iodoacetamidyl-3,6-dioxaoctanediamine-biotin, showed that Cys 161 is accessible from the outside in the carrier-CATR complex, whereas it is masked in the carrier-BA complex. Taken together, our results indicate that the matrix loop m2 connecting the transmembrane helices H3 to H4 intrudes to some extent into the inner mitochondrial membrane. Its participation in the translocation of ADP/ATP is strongly suggested, based on the finding that its accessibility to reagents added outside mitochondria is modified according to the conformational state of the carrier.
    MeSH term(s) Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Atractyloside/analogs & derivatives ; Atractyloside/metabolism ; Bongkrekic Acid/metabolism ; Mitochondria/metabolism ; Mitochondrial ADP, ATP Translocases/antagonists & inhibitors ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/metabolism ; Protein Conformation ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/antagonists & inhibitors ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Structure-Activity Relationship
    Chemical Substances PET9 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Bongkrekic Acid (11076-19-0) ; Atractyloside (17754-44-8) ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Mitochondrial ADP, ATP Translocases (9068-80-8) ; carboxyatractyloside (SNP1XL23E6)
    Language English
    Publishing date 2005-12-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi0514820
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  7. Article: Molecular, functional, and pathological aspects of the mitochondrial ADP/ATP carrier.

    Dahout-Gonzalez, C / Nury, H / Trézéguet, V / Lauquin, G J-M / Pebay-Peyroula, E / Brandolin, G

    Physiology (Bethesda, Md.)

    2006  Volume 21, Page(s) 242–249

    Abstract: In providing the cell with ATP generated by oxidative phosphorylation, the mitochondrial ADP/ATP carrier plays a central role in aerobic eukaryotic cells. Combining biochemical, genetic, and structural approaches contributes to understanding the ... ...

    Abstract In providing the cell with ATP generated by oxidative phosphorylation, the mitochondrial ADP/ATP carrier plays a central role in aerobic eukaryotic cells. Combining biochemical, genetic, and structural approaches contributes to understanding the molecular mechanism of this essential transport system, the dysfunction of which is implicated in neuromuscular diseases.
    MeSH term(s) Animals ; Atractyloside/analogs & derivatives ; Atractyloside/chemistry ; Atractyloside/pharmacology ; Cell Respiration/physiology ; Gene Expression/drug effects ; Gene Expression/physiology ; Humans ; Mitochondria, Muscle/physiology ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/physiology ; Neuromuscular Diseases/physiopathology
    Chemical Substances Atractyloside (17754-44-8) ; Mitochondrial ADP, ATP Translocases (9068-80-8) ; carboxyatractyloside (SNP1XL23E6)
    Language English
    Publishing date 2006-08
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2158667-6
    ISSN 1548-9221 ; 1548-9213
    ISSN (online) 1548-9221
    ISSN 1548-9213
    DOI 10.1152/physiol.00005.2006
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  8. Article: Relations between structure and function of the mitochondrial ADP/ATP carrier.

    Nury, H / Dahout-Gonzalez, C / Trézéguet, V / Lauquin, G J M / Brandolin, G / Pebay-Peyroula, E

    Annual review of biochemistry

    2006  Volume 75, Page(s) 713–741

    Abstract: Import and export of metabolites through mitochondrial membranes are vital processes that are highly controlled and regulated at the level of the inner membrane. Proteins of the mitochondrial carrier family ( MCF ) are embedded in this membrane, and each ...

    Abstract Import and export of metabolites through mitochondrial membranes are vital processes that are highly controlled and regulated at the level of the inner membrane. Proteins of the mitochondrial carrier family ( MCF ) are embedded in this membrane, and each member of the family achieves the selective transport of a specific metabolite. Among these, the ADP/ATP carrier transports ADP into the mitochondrial matrix and exports ATP toward the cytosol after its synthesis. Because of its natural abundance, the ADP/ATP carrier is the best characterized within MCF, and a high-resolution structure of one conformation is known. The overall structure is basket shaped and formed by six transmembrane helices that are not only tilted with respect to the membrane, but three of them are also kinked at the level of prolines. The functional mechanisms, nucleotide recognition, and conformational changes for the transport, suggested from the structure, are discussed along with the large body of biochemical and functional results.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Humans ; Lipids/chemistry ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/genetics ; Mitochondrial ADP, ATP Translocases/metabolism ; Mitochondrial Membranes/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleotides/chemistry ; Nucleotides/metabolism ; Protein Conformation ; Structure-Activity Relationship
    Chemical Substances Lipids ; Nucleotides ; Adenosine Triphosphate (8L70Q75FXE) ; Mitochondrial ADP, ATP Translocases (9068-80-8)
    Language English
    Publishing date 2006
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev.biochem.75.103004.142747
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  9. Article ; Online: Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside.

    Pebay-Peyroula, Eva / Dahout-Gonzalez, Cécile / Kahn, Richard / Trézéguet, Véronique / Lauquin, Guy J-M / Brandolin, Gérard

    Nature

    2003  Volume 426, Issue 6962, Page(s) 39–44

    Abstract: ATP, the principal energy currency of the cell, fuels most biosynthetic reactions in the cytoplasm by its hydrolysis into ADP and inorganic phosphate. Because resynthesis of ATP occurs in the mitochondrial matrix, ATP is exported into the cytoplasm while ...

    Abstract ATP, the principal energy currency of the cell, fuels most biosynthetic reactions in the cytoplasm by its hydrolysis into ADP and inorganic phosphate. Because resynthesis of ATP occurs in the mitochondrial matrix, ATP is exported into the cytoplasm while ADP is imported into the matrix. The exchange is accomplished by a single protein, the ADP/ATP carrier. Here we have solved the bovine carrier structure at a resolution of 2.2 A by X-ray crystallography in complex with an inhibitor, carboxyatractyloside. Six alpha-helices form a compact transmembrane domain, which, at the surface towards the space between inner and outer mitochondrial membranes, reveals a deep depression. At its bottom, a hexapeptide carrying the signature of nucleotide carriers (RRRMMM) is located. Our structure, together with earlier biochemical results, suggests that transport substrates bind to the bottom of the cavity and that translocation results from a transient transition from a 'pit' to a 'channel' conformation.
    MeSH term(s) Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Atractyloside/analogs & derivatives ; Atractyloside/chemistry ; Atractyloside/metabolism ; Atractyloside/pharmacology ; Binding Sites ; Cattle ; Crystallography, X-Ray ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/metabolism ; Enzyme Inhibitors/pharmacology ; Mitochondrial ADP, ATP Translocases/antagonists & inhibitors ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial ADP, ATP Translocases/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Static Electricity
    Chemical Substances Enzyme Inhibitors ; Atractyloside (17754-44-8) ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Mitochondrial ADP, ATP Translocases (9068-80-8) ; carboxyatractyloside (SNP1XL23E6)
    Language English
    Publishing date 2003-11-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature02056
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  10. Article: An optimized strategy for ICAT quantification of membrane proteins.

    Ramus, Claire / Gonzalez de Peredo, Anne / Dahout, Cécile / Gallagher, Maighread / Garin, Jérôme

    Molecular & cellular proteomics : MCP

    2005  Volume 5, Issue 1, Page(s) 68–78

    Abstract: The work presented here focuses on the development of a method adapting isotope labeling of proteins with ICAT to the study of highly hydrophobic proteins. Conditions for the labeling of proteins were first established using two standard soluble proteins ...

    Abstract The work presented here focuses on the development of a method adapting isotope labeling of proteins with ICAT to the study of highly hydrophobic proteins. Conditions for the labeling of proteins were first established using two standard soluble proteins and iodoacetamidyl-3,6-dioxaoctanediamine biotin (PEO-iodoacetyl biotin). Results demonstrated the efficiency of the labeling in the presence of high concentrations of both SDS and urea. These conditions were then used to label a highly hydrophobic mitochondrial membrane protein, the adenine nucleotide translocator ANT-1, with PEO-iodoacetyl biotin and then with the cleavable ICAT reagent. The results presented here show that labeling of proteins with cleavable ICAT is possible and may even be improved in strong denaturing buffers containing both SDS at a concentration higher than 0.5% (w/v) and urea. These results open the possibility of applying the ICAT strategy to complex samples containing very hydrophobic proteins solubilized in urea-SDS buffers. The adaptability of the developed method is demonstrated here with preliminary results obtained during the study of membrane-enriched fractions prepared from murine embryonic stem cells.
    MeSH term(s) Affinity Labels ; Animals ; Biotin/chemistry ; Cattle ; Chickens ; Cysteine/chemistry ; Electrophoresis, Gel, Two-Dimensional ; Embryo, Mammalian/cytology ; Embryo, Mammalian/metabolism ; Embryo, Nonmammalian ; Isotope Labeling ; Lactoglobulins/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Mice ; Ovalbumin/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Stem Cells/metabolism ; Trypsin/metabolism ; Urea/metabolism
    Chemical Substances Affinity Labels ; Lactoglobulins ; Membrane Proteins ; Biotin (6SO6U10H04) ; Urea (8W8T17847W) ; Ovalbumin (9006-59-1) ; Trypsin (EC 3.4.21.4) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2005-10-10
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2075924-1
    ISSN 1535-9484 ; 1535-9476
    ISSN (online) 1535-9484
    ISSN 1535-9476
    DOI 10.1074/mcp.M500205-MCP200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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