Abstract
An ATX1 homologue of 503 bp length was cloned from a rat cDNA library, and the deduced protein from the cDNA was found to contain 68 amino acids with a predicted molecular mass of 7.2 kDa. The rat ATX1 homologue protein (Rah1p), which shows 35%, 38%, and 89% identities with Atx1p, CUC-1, and HAH1, respectively, conserves both the MTCXXC copper-binding site in the N terminus and the KTGK lysine-rich region in the C terminus. In Northern blot analysis, rah1 mRNA was found to be expressed at high levels in the liver, small intestine, and testis. Expression of rah1 cDNA complemented a null atx1 mutant strain in yeast. Thus, Rah1p was concluded to be a functional copper chaperone.
Copyright 1999 Academic Press.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Carrier Proteins*
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Cloning, Molecular
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Copper / metabolism
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Copper Transport Proteins
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DNA Primers / genetics
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DNA, Complementary / genetics
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DNA, Complementary / isolation & purification
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Fungal Proteins / genetics*
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Genetic Complementation Test
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Male
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Molecular Chaperones / genetics*
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Molecular Chaperones / metabolism
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Molecular Sequence Data
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Mutation
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Rats
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Rats, Sprague-Dawley
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Tissue Distribution
Substances
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ATX1 protein, S cerevisiae
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Atox1 protein, rat
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Carrier Proteins
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Copper Transport Proteins
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DNA Primers
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DNA, Complementary
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Fungal Proteins
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Molecular Chaperones
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RNA, Messenger
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Saccharomyces cerevisiae Proteins
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Copper