Closing Plant Stomata Requires a Homolog of an Aluminum-Activated Malate Transporter

被引:148
作者
Sasaki, Takayuki [1 ]
Mori, Izumi C. [1 ]
Furuichi, Takuya [1 ]
Munemasa, Shintaro [2 ]
Toyooka, Kiminori [3 ]
Matsuoka, Ken [4 ]
Murata, Yoshiyuki [2 ]
Yamamoto, Yoko [1 ]
机构
[1] Okayama Univ, Bioresources Res Inst, Okayama 7100046, Japan
[2] Okayama Univ, Grad Sch Nat Sci & Technol, Okayama 7008530, Japan
[3] RIKEN Plant Sci Ctr, Tsurumi Ku, Yokohama, Kanagawa 2300045, Japan
[4] Kyushu Univ, Lab Plant Nutr, Fac Agr, Fukuoka 8128581, Japan
关键词
ALMT family protein; Anion transporter; AtALMT12; Stomatal closure; SLOW ANION CHANNELS; ABSCISIC-ACID; GUARD-CELLS; K+ CHANNEL; PLASMA-MEMBRANE; XENOPUS OOCYTES; ION CHANNELS; ARABIDOPSIS; TOLERANCE; PROTEIN;
D O I
10.1093/pcp/pcq016
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Plant stomata limit both carbon dioxide uptake and water loss; hence, stomatal aperture is carefully set as the environment fluctuates. Aperture area is known to be regulated in part by ion transport, but few of the transporters have been characterized. Here we report that AtALMT12 (At4g17970), a homolog of the aluminum-activated malate transporter (ALMT) of wheat, is expressed in guard cells of Arabidopsis thaliana. Loss-of-function mutations in AtALMT12 impair stomatal closure induced by ABA, calcium and darkness, but do not abolish either the rapidly activated or the slowly activated anion currents previously identified as being important for stomatal closure. Expressed in Xenopus oocytes, AtALMT12 facilitates chloride and nitrate currents, but not those of organic solutes. Therefore, we conclude that AtALMT12 is a novel class of anion transporter involved in stomatal closure.
引用
收藏
页码:354 / 365
页数:12
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