Chromosomal localization and genomic structure of the human arsenite-stimulated ATPase (hASNA-I).
The hASNA-I is a novel human arsenite-stimulated ATPase identified as the human paralogue of the ATPase component of the arsenite efflux system in E. coli. The hASNA-I has distinct biochemical properties and a dual nuclear and cytoplasmic distribution. Immunohistochemical staining showed a distinct pattern of hASNA-I expression in cells within normal tissues, and its overexpression in breast cancer. Recently, the yeast two-hybrid system has identified hASNA-I as a cellular partner of metallothionein II suggesting an additional role in Zn homeostasis and cellular detoxification. This report describes the assignment of hASNA-I to human chromosome 19 by somatic-cell hybrid PCR mapping, the isolation of a chromosome 19-specific cosmid clone, and the genomic structure and exon-intron boundaries of hASNA-I. Our results indicate that the coding region of hASNA-I consists of 4 exons spanning 6 kb on band 19q13.3. These data will facilitate molecular analysis of the role of hASNA-I in human disease.
Kurdi-Haidar
B
B
Department of Medicine, University of California San Diego, La Jolla 92093-0058, USA.
Heath
D
D
Lennon
G
G
Howell
S B
SB
D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000378:metabolism; D053501:Arsenite Transporting ATPases; D018053:Arsenites / Q000494:pharmacology; D002874:Chromosome Mapping / Q000379:methods; D002888:Chromosomes, Human, Pair 19 / Q000235:genetics; D003360:Cosmids / Q000235:genetics; D020536:Enzyme Activators / Q000494:pharmacology; D005091:Exons / Q000235:genetics; D015698:Genomic Library; D006801:Humans; D007438:Introns / Q000235:genetics; D016623:Ion Pumps; D009097:Multienzyme Complexes; D015183:Restriction Mapping; D013723:Teratogens / Q000494:pharmacology
D018053:Arsenites; D020536:Enzyme Activators; D016623:Ion Pumps; D009097:Multienzyme Complexes; D013723:Teratogens; D000251:Adenosine Triphosphatases; D053501:Arsenite Transporting ATPases; C015001:arsenite