Rice P-1B-type heavy-metal ATPase, OsHMA9, is a metal efflux protein
SCIE
SCOPUS
- Title
- Rice P-1B-type heavy-metal ATPase, OsHMA9, is a metal efflux protein
- Authors
- Lee, S; Kim, YY; Lee, Y; An, G
- Date Issued
- 2007-11
- Publisher
- AMER SOC PLANT BIOLOGISTS
- Abstract
- P-1B-type heavy-metal ATPases (HMAs) are transmembrane metal- transporting proteins that play a key role in metal homeostasis. Despite their importance, very little is known about their functions in monocot species. We report the characterization of rice (Oryza sativa) OsHMA9, a member of the P (1B)- type ATPase family. Semiquantitative reverse transcription- polymerase chain reaction analyses of seedlings showed that OsHMA9 expression was induced by a high concentration of copper (Cu), zinc (Zn), and cadmium. We also determined, through promoter:: beta- glucuronidase analysis, that the main expression was in the vascular bundles and anthers. The OsHMA9: green fluorescence protein fusion was localized to the plasma membrane. Heterologous expression of OsHMA9 partially rescued the Cu sensitivity of the Escherichia coli copA mutant, which is defective in Cu- transporting ATPases. It did not rescue the Zn sensitivity of the zntA mutant, which is defective in Zn- transporting ATPase. To further elucidate the functional roles of OsHMA9, we isolated two independent null alleles, oshma9- 1 and oshma9-2, from the T- DNA insertion population. Mutant plants exhibited the phenotype of increased sensitivity to elevated levels of Cu, Zn, and lead. These results support a role for OsHMA9 in Cu, Zn, and lead efflux from the cells. This article is the first report on the functional characterization of a P-1B- type metal efflux transporter in monocots.
- Keywords
- P-TYPE ATPASE; DNA INSERTIONAL MUTAGENESIS; ARABIDOPSIS-THALIANA; TAGGING LINES; FUNCTIONAL EXPRESSION; TRANSPORTING ATPASES; COPPER TRANSPORTER; DRAFT SEQUENCE; ION PUMPS; PLANTS
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/23086
- DOI
- 10.1104/PP.107.10223
- ISSN
- 0032-0889
- Article Type
- Article
- Citation
- PLANT PHYSIOLOGY, vol. 145, no. 3, page. 831 - 842, 2007-11
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