Chromosomal localization and genomic structure of the human arsenite-stimulated ATPase (hASNA-I)

Somat Cell Mol Genet. 1998 Sep;24(5):307-11. doi: 10.1023/b:scam.0000007134.16744.8b.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / genetics*
  • Adenosine Triphosphatases / metabolism
  • Arsenite Transporting ATPases
  • Arsenites / pharmacology
  • Chromosome Mapping* / methods
  • Chromosomes, Human, Pair 19 / genetics
  • Cosmids / genetics
  • Enzyme Activators / pharmacology
  • Exons / genetics
  • Genomic Library
  • Humans
  • Introns / genetics
  • Ion Pumps*
  • Multienzyme Complexes*
  • Restriction Mapping
  • Teratogens / pharmacology

Substances

  • Arsenites
  • Enzyme Activators
  • Ion Pumps
  • Multienzyme Complexes
  • Teratogens
  • Adenosine Triphosphatases
  • Arsenite Transporting ATPases
  • arsenite