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Published on August 13, 2008; 10.1104/pp.108.119933

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Received April 8, 2008
Accepted August 8, 2008

Amino Acid Polymorphisms in Strictly Conserved Domains of a P-type ATPase HMA5 are Involved in the Mechanism of Copper Tolerance Variation in Arabidopsis

Yuriko Kobayashi , Keishi Kuroda , Keisuke Kimura , Jennafer L. Southron-Francis , Aya Furuzawa , Kazuhiko Kimura , Satoshi Iuchi , Masatomo Kobayashi , Gregory J. Taylor , and Hiroyuki Koyama *

Laboratory of Plant Cell Technology, Faculty of Applied Biological Sciences, Gifu University, 501-1193, Gifu, Japan; Department of Farm Management, Miyagi University, 981-3298, Sendai, Miyagi, Japan; Department of Biological Sciences, Faculty of Science, University of Alberta, T6G 2E9, Edmonton, Alberta, Canada; BioResource Center, RIKEN, 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan

* Corresponding author; email: koyama{at}gifu-u.ac.jp.

Copper (Cu) is an essential element in plant nutrition, but it inhibits growth of roots at low concentrations. Accessions of Arabidopsis (Arabidopsis thaliana) vary in their tolerance to Cu. To understand the molecular mechanism of Cu tolerance in Arabidopsis, we performed QTL analysis and accession studies. One major QTL on chromosome 1 (QTL1) explained 52% of the phenotypic variation in Cu tolerance in roots in a Ler/Cvi recombinant inbred population. This QTL regulates Cu translocation capacity and involves a Cu-transporting P1B-1-type ATPase, HMA5. The Cvi allele carries two amino acid substitutions in comparison with the Ler allele and is less functional than the Ler allele in Cu tolerance when judged by complementation assays using a T-DNA insertion mutant. Complementation assays of the ccc2 mutant of yeast using chimeric HMA5 proteins revealed that N923T of the Cvi allele, which was identified in the tightly conserved domain N(x)6YN(x)4P (where the former asparagine was substituted to threonine), is a cause of dysfunction of the Cvi HMA5 allele. Another dysfunctional HMA5 allele was identified in Chisdra-2 (Chi-2), which showed Cu sensitivity and low capacity of Cu translocation from roots to shoots. A unique amino acid substitution of Chi-2 was identified in another strictly conserved domain, CPC(x)6P, where the latter proline was replaced with leucine. These results indicate that a portion of the variation in Cu tolerance of Arabidospsis is regulated by functional integrity of the Cu-translocating ATPase, HMA5, and in particular to the amino acid sequence in several strictly conserved motifs.




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