The mitochondrial ABC transporter Atm1p functions as a homodimer

The ATP-binding cassette (ABC) transporters constitute one of the largest families of proteins in evolution. The ATM1 gene of the yeast Saccharomyces cerevisiae encodes an ABC protein, which is localized to the mitochondrial inner membrane. A deletion of ATM1 results in the accumulation of up to a 3...

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Bibliographic Details
Published in:	FEBS letters Vol. 569; no. 1-3; pp. 65 - 69
Main Authors:	Chloupková, Maja, Reaves, Scott K, LeBard, Linda M, Koeller, David M
Format:	Journal Article
Language:	English
Published:	England Elsevier B.V 02-07-2004
Subjects:	ABC transporter ABC, ATP-binding cassette Amino Acid Sequence ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Base Sequence CFTR, cystic fibrosis transmembrane conductance regulator Conserved Sequence Dimerization DNA Primers Fe-S protein Genetic Complementation Test HC, Hartwell's complete medium IP, immunoprecipitation Iron metabolism Mitochondria - metabolism Mitochondrion Molecular Sequence Data Mutagenesis, Site-Directed NBD, nucleotide binding domain Plasmids Recombinant Proteins - chemistry Recombinant Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sequence Alignment TMD, transmembrane domain Mitochondrion NBD ABC Iron metabolism IP Fe-S protein TMD HC ABC transporter CFTR
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Summary:	The ATP-binding cassette (ABC) transporters constitute one of the largest families of proteins in evolution. The ATM1 gene of the yeast Saccharomyces cerevisiae encodes an ABC protein, which is localized to the mitochondrial inner membrane. A deletion of ATM1 results in the accumulation of up to a 30-fold excess of mitochondrial iron, loss of mitochondrial cytochromes and abnormalities of cytosolic iron metabolism. In this study, we have evaluated the role of conserved sequence elements in Atm1p in its function and dimerization in vivo. We report that conserved residues in the Walker A and B motifs of the nucleotide binding domain, which are required for ATP binding and hydrolysis, are essential for Atm1p function. In addition, we provide evidence that ATP binding is important for Atm1p dimerization.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2004.05.051