Abstract
Acid soil syndrome causes severe yield losses in various crop plants because of the rhizotoxicities of ions, such as aluminum (Al3+). Although protons (H+) could be also major rhizotoxicants in some soil types, molecular mechanisms of their tolerance have not been identified yet. One mutant that was hypersensitive to H+ rhizotoxicity was isolated from ethyl methanesulfonate mutagenized seeds, and a single recessive mutation was found on chromosome 1. Positional cloning followed by genomic sequence analysis revealed that a missense mutation in the zinc finger domain in a predicted Cys2His2-type zinc finger protein, namely sensitive to proton rhizotoxicity (STOP)1, is the cause of hypersensitivity to H+ rhizotoxicity. The STOP1 protein belongs to a functionally unidentified subfamily of zinc finger proteins, which consists of two members in Arabidopsis based on a Blast search. The stop1 mutation resulted in no effects on cadmium, copper, lanthanum, manganese and sodium chloride sensitivitities, whereas it caused hypersensitivity to Al3+ rhizotoxicity. This stop1 mutant lacked the induction of the AtALMT1 gene encoding a malate transporter, which is concomitant with Al-induced malate exudation. There was no induction of AtALMT1 by Al3+ treatment in the stop1 mutant. These results indicate that STOP1 plays a critical role in Arabidopsis tolerance to major stress factors in acid soils.
| Original language | English |
|---|---|
| Pages (from-to) | 9900-9905 |
| Number of pages | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 104 |
| Issue number | 23 |
| DOIs | |
| Publication status | Published - Jun 5 2007 |
| Externally published | Yes |
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Keywords
- Aluminum toxicity
- Arabidopsis thaliana
- CysHis-type zinc finger protein
- Proton-rhizotoxicity
- Sensitive to proton rhizotoxicity
ASJC Scopus subject areas
- Genetics
- General
Cite this
Zinc finger protein STOP1 is critical for proton tolerance in Arabidopsis and coregulates a key gene in aluminum tolerance. / Iuchi, Satoshi; Koyama, Hiroyuki; Iuchi, Atsuko; Kobayashi, Yasufumi; Kitabayashi, Sadako; Kobayashi, Yuriko; Ikka, Takashi; Hirayama, Takashi; Shinozaki, Kazuo; Kobayashi, Masatomo.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, No. 23, 05.06.2007, p. 9900-9905.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Zinc finger protein STOP1 is critical for proton tolerance in Arabidopsis and coregulates a key gene in aluminum tolerance
AU - Iuchi, Satoshi
AU - Koyama, Hiroyuki
AU - Iuchi, Atsuko
AU - Kobayashi, Yasufumi
AU - Kitabayashi, Sadako
AU - Kobayashi, Yuriko
AU - Ikka, Takashi
AU - Hirayama, Takashi
AU - Shinozaki, Kazuo
AU - Kobayashi, Masatomo
PY - 2007/6/5
Y1 - 2007/6/5
N2 - Acid soil syndrome causes severe yield losses in various crop plants because of the rhizotoxicities of ions, such as aluminum (Al3+). Although protons (H+) could be also major rhizotoxicants in some soil types, molecular mechanisms of their tolerance have not been identified yet. One mutant that was hypersensitive to H+ rhizotoxicity was isolated from ethyl methanesulfonate mutagenized seeds, and a single recessive mutation was found on chromosome 1. Positional cloning followed by genomic sequence analysis revealed that a missense mutation in the zinc finger domain in a predicted Cys2His2-type zinc finger protein, namely sensitive to proton rhizotoxicity (STOP)1, is the cause of hypersensitivity to H+ rhizotoxicity. The STOP1 protein belongs to a functionally unidentified subfamily of zinc finger proteins, which consists of two members in Arabidopsis based on a Blast search. The stop1 mutation resulted in no effects on cadmium, copper, lanthanum, manganese and sodium chloride sensitivitities, whereas it caused hypersensitivity to Al3+ rhizotoxicity. This stop1 mutant lacked the induction of the AtALMT1 gene encoding a malate transporter, which is concomitant with Al-induced malate exudation. There was no induction of AtALMT1 by Al3+ treatment in the stop1 mutant. These results indicate that STOP1 plays a critical role in Arabidopsis tolerance to major stress factors in acid soils.
AB - Acid soil syndrome causes severe yield losses in various crop plants because of the rhizotoxicities of ions, such as aluminum (Al3+). Although protons (H+) could be also major rhizotoxicants in some soil types, molecular mechanisms of their tolerance have not been identified yet. One mutant that was hypersensitive to H+ rhizotoxicity was isolated from ethyl methanesulfonate mutagenized seeds, and a single recessive mutation was found on chromosome 1. Positional cloning followed by genomic sequence analysis revealed that a missense mutation in the zinc finger domain in a predicted Cys2His2-type zinc finger protein, namely sensitive to proton rhizotoxicity (STOP)1, is the cause of hypersensitivity to H+ rhizotoxicity. The STOP1 protein belongs to a functionally unidentified subfamily of zinc finger proteins, which consists of two members in Arabidopsis based on a Blast search. The stop1 mutation resulted in no effects on cadmium, copper, lanthanum, manganese and sodium chloride sensitivitities, whereas it caused hypersensitivity to Al3+ rhizotoxicity. This stop1 mutant lacked the induction of the AtALMT1 gene encoding a malate transporter, which is concomitant with Al-induced malate exudation. There was no induction of AtALMT1 by Al3+ treatment in the stop1 mutant. These results indicate that STOP1 plays a critical role in Arabidopsis tolerance to major stress factors in acid soils.
KW - Aluminum toxicity
KW - Arabidopsis thaliana
KW - CysHis-type zinc finger protein
KW - Proton-rhizotoxicity
KW - Sensitive to proton rhizotoxicity
UR - http://www.scopus.com/inward/record.url?scp=34547453356&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34547453356&partnerID=8YFLogxK
U2 - 10.1073/pnas.0700117104
DO - 10.1073/pnas.0700117104
M3 - Article
VL - 104
SP - 9900
EP - 9905
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 23
ER -