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Isolation of the AT...
Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter.
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Kurdi-Haidar, B (author)
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Aebi, S (author)
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Heath, D (author)
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Enns, R E (author)
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- Naredi, Peter, 1955 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för de kirurgiska disciplinerna, Avdelningen för kirurgi,Institute of Surgical Sciences, Department of Surgery
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Hom, D K (author)
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Howell, S B (author)
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(creator_code:org_t)
- Elsevier BV, 1996
- 1996
- English.
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In: Genomics. - : Elsevier BV. - 0888-7543. ; 36:3, s. 486-91
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https://doi.org/10.1...
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Abstract
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- 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)
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