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The mitochondrial ABC transporter Atm1p functions as a homodimer
Author(s) -
Chloupková Maja,
Reaves Scott K,
LeBard Linda M,
Koeller David M
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.051
Subject(s) - saccharomyces cerevisiae , atp binding cassette transporter , atp hydrolysis , biochemistry , transporter , inner mitochondrial membrane , mitochondrion , yeast , cytosol , cyclic nucleotide binding domain , mitochondrial carrier , function (biology) , biology , binding site , conserved sequence , nucleotide , walker motifs , chemistry , microbiology and biotechnology , gene , atpase , peptide sequence , bacterial outer membrane , enzyme , escherichia coli
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.