Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter.
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Kurdi-Haidar B, Aebi S, Heath D, Enns RE, Naredi P, Hom DK, Howell SB
Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter.
Genomics. 1996 Sep 15;36(3):486-91.
- PubMed ID
- 8884272 [ View in PubMed]
- Abstract
Arsenite resistance in bacteria is mediated by an efflux pump composed of the arsA and arsB gene products. We have isolated the human homolog of the bacterial arsA (hARSA-I), a member of the ATPase superfamily with no transmembrane domain. Southern and Northern analyses indicated the presence of two cross-hybridizing genes in the human genome and expression of hARSA-I in many tissues. A rabbit antiserum raised against a glutathione-S-transferase (GST)/hARSA-I fusion protein identified two cross-reacting proteins of 37 and 42 kDa by Western analysis in two different human cell lines. Overexpression of hARSA-I in the embryonal human kidney 293 cell line was accompanied by overproduction of the 37-kDa protein Biochemical analysis using the GST/hARSA-I fusion protein indicated that hARSA-I is an ATPase analogous to the bacterial ArsA. Thus, hARSA-I is a new eukaryotic member of a highly conserved ATP-binding superfamily of proteins.