Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations

博士 === 國防醫學院 === 生命科學研究所 === 97 === Ions, essential nutrients for higher plants, also act as signal molecules. Little is known about how plants sense changes in soil nutrient concentrations. In this study, analysis of an uptake- and sensing-decoupled mutant showed that the dual-affinity nitrate tra...

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Main Authors: CHENG HSUN HO, 何承訓
Other Authors: Yi-Fang Tsay
Format: Others
Language:en_US
Published: 2009
Online Access:http://ndltd.ncl.edu.tw/handle/86148129177809084600
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spelling ndltd-TW-097NDMC01050262016-05-06T04:11:48Z http://ndltd.ncl.edu.tw/handle/86148129177809084600 Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations 硝酸鹽感應子CHL1受到磷酸激酶CIPK23的調控而偵測土壤中硝酸鹽濃度變化作用機制之研究 CHENG HSUN HO 何承訓 博士 國防醫學院 生命科學研究所 97 Ions, essential nutrients for higher plants, also act as signal molecules. Little is known about how plants sense changes in soil nutrient concentrations. In this study, analysis of an uptake- and sensing-decoupled mutant showed that the dual-affinity nitrate transporter CHL1 functions as a nitrate sensor. Previous studies showed that T101-phosphorylated CHL1 is a high-affinity nitrate transporter, while T101-dephosphorylated CHL1 is a low-affinity transporter. Here, primary nitrate responses in CHL1T101D and CHLT101A transgenic plants showed that the phosphorylated and dephosphorylated CHL1 lead to a low- and high-level response, respectively. In vitro and in vivo studies showed that, in response to low nitrate concentrations, protein kinase CIPK23 can phosphorylate T101 of CHL1 to maintain a low-level primary response. CHL1, the first ion sensor identified in higher plants, uses dual-affinity binding and phosphorylation switching to sense a wide range of nitrate concentrations in the soil and thus trigger different levels of nitrate response. Yi-Fang Tsay 蔡宜芳 2009 學位論文 ; thesis 0 en_US
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language en_US
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description 博士 === 國防醫學院 === 生命科學研究所 === 97 === Ions, essential nutrients for higher plants, also act as signal molecules. Little is known about how plants sense changes in soil nutrient concentrations. In this study, analysis of an uptake- and sensing-decoupled mutant showed that the dual-affinity nitrate transporter CHL1 functions as a nitrate sensor. Previous studies showed that T101-phosphorylated CHL1 is a high-affinity nitrate transporter, while T101-dephosphorylated CHL1 is a low-affinity transporter. Here, primary nitrate responses in CHL1T101D and CHLT101A transgenic plants showed that the phosphorylated and dephosphorylated CHL1 lead to a low- and high-level response, respectively. In vitro and in vivo studies showed that, in response to low nitrate concentrations, protein kinase CIPK23 can phosphorylate T101 of CHL1 to maintain a low-level primary response. CHL1, the first ion sensor identified in higher plants, uses dual-affinity binding and phosphorylation switching to sense a wide range of nitrate concentrations in the soil and thus trigger different levels of nitrate response.
author2 Yi-Fang Tsay
author_facet Yi-Fang Tsay
CHENG HSUN HO
何承訓
author CHENG HSUN HO
何承訓
spellingShingle CHENG HSUN HO
何承訓
Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations
author_sort CHENG HSUN HO
title Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations
title_short Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations
title_full Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations
title_fullStr Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations
title_full_unstemmed Nitrate sensor CHL1, regulated by protein kinase CIPK23, detects a wide range of soil nitrate concentrations
title_sort nitrate sensor chl1, regulated by protein kinase cipk23, detects a wide range of soil nitrate concentrations
publishDate 2009
url http://ndltd.ncl.edu.tw/handle/86148129177809084600
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