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The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol

Standard

The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. / Metz, Jutta; Wächter, Andrea; Schmidt, Bastian; Bujnicki, Janusz M; Schwappach, Blanche.

in: J BIOL CHEM, Jahrgang 281, Nr. 1, 06.01.2006, S. 410-7.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Metz, J, Wächter, A, Schmidt, B, Bujnicki, JM & Schwappach, B 2006, 'The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol', J BIOL CHEM, Jg. 281, Nr. 1, S. 410-7. https://doi.org/10.1074/jbc.M507481200

APA

Metz, J., Wächter, A., Schmidt, B., Bujnicki, J. M., & Schwappach, B. (2006). The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J BIOL CHEM, 281(1), 410-7. https://doi.org/10.1074/jbc.M507481200

Vancouver

Metz J, Wächter A, Schmidt B, Bujnicki JM, Schwappach B. The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J BIOL CHEM. 2006 Jan 6;281(1):410-7. https://doi.org/10.1074/jbc.M507481200

Bibtex

@article{1840b514aefb4c1f9f3a7b201c2a3597,
title = "The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol",
abstract = "Cellular ion homeostasis involves communication between the cytosol and the luminal compartment of organelles. This is particularly critical for metal ions because of their toxic potential. We have identified the yeast homologue of the prokaryotic ArsA protein, the homodimeric ATPase Arr4p, as a protein that binds to the yeast intracellular CLC chloride-transport protein, Gef1p. We show that binding of Arr4p to the C terminus of Gef1p requires the presence of yeast cytosol and is sensitive to a highly specific copper chelator in vitro and in vivo. Copper alone can substitute for cytosol to support the interaction of Arr4p with the C terminus of Gef1p. The migration behavior of Arr4p in nonreducing gel electrophoresis correlates with cellular copper deficiency, repletion, or stress. Our homology model of Arr4p shows that the antimony (arsenic) metal binding site of ArsA is not conserved in Arr4p. The model suggests that a pair of cysteines, Cys285 and Cys288, is located in the interface of the Arr4p dimer. These residues are required for Arr4p homodimerization and for binding to the C terminus of Gef1p. Whereas both proteins are required for normal growth under iron-limiting conditions, they play opposite roles when copper and heat stress are combined in an alkaline environment. Under these conditions, deltagef1 cells grow much better than wild type yeast, whereas deltaarr4 cells are unable to grow. Comparison of the deltaarr4 with the deltaarr4deltagef1 strain suggests that Arr4p antagonizes the function of Gef1p.",
keywords = "Adenosine Triphosphatases/chemistry, Animals, Antibodies, Arsenate Reductases, Arsenite Transporting ATPases, Chloride Channels/metabolism, Chlorides/metabolism, Copper/metabolism, Cytosol/metabolism, Dimerization, Guinea Pigs, Heat-Shock Response, Ion Pumps, Multienzyme Complexes, Protein Structure, Secondary, Protein Structure, Tertiary, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/metabolism",
author = "Jutta Metz and Andrea W{\"a}chter and Bastian Schmidt and Bujnicki, {Janusz M} and Blanche Schwappach",
year = "2006",
month = jan,
day = "6",
doi = "10.1074/jbc.M507481200",
language = "English",
volume = "281",
pages = "410--7",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol

AU - Metz, Jutta

AU - Wächter, Andrea

AU - Schmidt, Bastian

AU - Bujnicki, Janusz M

AU - Schwappach, Blanche

PY - 2006/1/6

Y1 - 2006/1/6

N2 - Cellular ion homeostasis involves communication between the cytosol and the luminal compartment of organelles. This is particularly critical for metal ions because of their toxic potential. We have identified the yeast homologue of the prokaryotic ArsA protein, the homodimeric ATPase Arr4p, as a protein that binds to the yeast intracellular CLC chloride-transport protein, Gef1p. We show that binding of Arr4p to the C terminus of Gef1p requires the presence of yeast cytosol and is sensitive to a highly specific copper chelator in vitro and in vivo. Copper alone can substitute for cytosol to support the interaction of Arr4p with the C terminus of Gef1p. The migration behavior of Arr4p in nonreducing gel electrophoresis correlates with cellular copper deficiency, repletion, or stress. Our homology model of Arr4p shows that the antimony (arsenic) metal binding site of ArsA is not conserved in Arr4p. The model suggests that a pair of cysteines, Cys285 and Cys288, is located in the interface of the Arr4p dimer. These residues are required for Arr4p homodimerization and for binding to the C terminus of Gef1p. Whereas both proteins are required for normal growth under iron-limiting conditions, they play opposite roles when copper and heat stress are combined in an alkaline environment. Under these conditions, deltagef1 cells grow much better than wild type yeast, whereas deltaarr4 cells are unable to grow. Comparison of the deltaarr4 with the deltaarr4deltagef1 strain suggests that Arr4p antagonizes the function of Gef1p.

AB - Cellular ion homeostasis involves communication between the cytosol and the luminal compartment of organelles. This is particularly critical for metal ions because of their toxic potential. We have identified the yeast homologue of the prokaryotic ArsA protein, the homodimeric ATPase Arr4p, as a protein that binds to the yeast intracellular CLC chloride-transport protein, Gef1p. We show that binding of Arr4p to the C terminus of Gef1p requires the presence of yeast cytosol and is sensitive to a highly specific copper chelator in vitro and in vivo. Copper alone can substitute for cytosol to support the interaction of Arr4p with the C terminus of Gef1p. The migration behavior of Arr4p in nonreducing gel electrophoresis correlates with cellular copper deficiency, repletion, or stress. Our homology model of Arr4p shows that the antimony (arsenic) metal binding site of ArsA is not conserved in Arr4p. The model suggests that a pair of cysteines, Cys285 and Cys288, is located in the interface of the Arr4p dimer. These residues are required for Arr4p homodimerization and for binding to the C terminus of Gef1p. Whereas both proteins are required for normal growth under iron-limiting conditions, they play opposite roles when copper and heat stress are combined in an alkaline environment. Under these conditions, deltagef1 cells grow much better than wild type yeast, whereas deltaarr4 cells are unable to grow. Comparison of the deltaarr4 with the deltaarr4deltagef1 strain suggests that Arr4p antagonizes the function of Gef1p.

KW - Adenosine Triphosphatases/chemistry

KW - Animals

KW - Antibodies

KW - Arsenate Reductases

KW - Arsenite Transporting ATPases

KW - Chloride Channels/metabolism

KW - Chlorides/metabolism

KW - Copper/metabolism

KW - Cytosol/metabolism

KW - Dimerization

KW - Guinea Pigs

KW - Heat-Shock Response

KW - Ion Pumps

KW - Multienzyme Complexes

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Saccharomyces cerevisiae/enzymology

KW - Saccharomyces cerevisiae Proteins/metabolism

U2 - 10.1074/jbc.M507481200

DO - 10.1074/jbc.M507481200

M3 - SCORING: Journal article

C2 - 16260785

VL - 281

SP - 410

EP - 417

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 1

ER -