Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter.
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.
Kurdi-Haidar
B
B
Department of Medicine, University of California San Diego, La Jolla 92093-0812, USA.
Aebi
S
S
Heath
D
D
Enns
R E
RE
Naredi
P
P
Hom
D K
DK
Howell
S B
SB
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D000595:Amino Acid Sequence; D053501:Arsenite Transporting ATPases; D002460:Cell Line; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D005982:Glutathione Transferase / Q000235:genetics; D006801:Humans; D007106:Immune Sera; D016623:Ion Pumps; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes; D009693:Nucleic Acid Hybridization; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism
D007106:Immune Sera; D016623:Ion Pumps; D009097:Multienzyme Complexes; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase; D000251:Adenosine Triphosphatases; D053501:Arsenite Transporting ATPases