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.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin -- Cancer och onkologi (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine -- Cancer and Oncology (hsv//eng)

Keyword

Adenosine Triphosphatases

genetics

immunology

metabolism

Amino Acid Sequence

Arsenite Transporting ATPases

Cell Line

Cloning

Molecular

Escherichia coli

genetics

Glutathione Transferase

genetics

Humans

Immune Sera

Ion Pumps

Molecular Sequence Data

Multienzyme Complexes

Nucleic Acid Hybridization

Recombinant Fusion Proteins

genetics

metabolism

Publication and Content Type

ref (subject category)

art (subject category)