The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>

<p>Abstract</p> <p>Background</p> <p>The ACT domain, named after bacterial aspartate kinase, chorismate mutase and TyrA (prephenate dehydrogenase), is a regulatory domain that serves as an amino acid-binding site in feedback-regulated amino acid metabolic enzymes. We ha...

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Main Authors: Hsu Chih-Ping, Chung Tsui-Yun, Sung Tzu-Ying, Hsieh Ming-Hsiun
Format: Article
Language:English
Published: BMC 2011-08-01
Series:BMC Plant Biology
Online Access:http://www.biomedcentral.com/1471-2229/11/118
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spelling doaj-69d2663898d94e07bf9049fc43e8ae942020-11-24T21:11:59ZengBMCBMC Plant Biology1471-22292011-08-0111111810.1186/1471-2229-11-118The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>Hsu Chih-PingChung Tsui-YunSung Tzu-YingHsieh Ming-Hsiun<p>Abstract</p> <p>Background</p> <p>The ACT domain, named after bacterial aspartate kinase, chorismate mutase and TyrA (prephenate dehydrogenase), is a regulatory domain that serves as an amino acid-binding site in feedback-regulated amino acid metabolic enzymes. We have previously identified a novel type of ACT domain-containing protein family, the ACT domain repeat (ACR) protein family, in <it>Arabidopsis</it>. Members of the ACR family, ACR1 to ACR8, contain four copies of the ACT domain that extend throughout the entire polypeptide. Here, we describe the identification of four novel ACT domain-containing proteins, namely ACR9 to ACR12, in <it>Arabidopsis</it>. The ACR9 and ACR10 proteins contain three copies of the ACT domain, whereas the ACR11 and ACR12 proteins have a putative transit peptide followed by two copies of the ACT domain. The functions of these plant ACR proteins are largely unknown.</p> <p>Results</p> <p>The ACR11 and ACR12 proteins are predicted to target to chloroplasts. We used protoplast transient expression assay to demonstrate that the <it>Arabidopsis </it>ACR11- and ACR12-green fluorescent fusion proteins are localized to the chloroplast. Analysis of an <it>ACR11 </it>promoter-β-glucuronidase (GUS) fusion in transgenic <it>Arabidopsis </it>revealed that the GUS activity was mainly detected in mature leaves and sepals. Interestingly, coexpression analysis revealed that the <it>GLN2</it>, which encodes a chloroplastic glutamine synthetase, has the highest mutual rank in the coexpressed gene network connected to <it>ACR11</it>. We used RNA gel blot analysis to confirm that the expression pattern of <it>ACR11 </it>is similar to that of <it>GLN2 </it>in various organs from 6-week-old <it>Arabidopsis</it>. Moreover, the expression of <it>ACR11 </it>and <it>GLN2 </it>is highly co-regulated by sucrose and light/dark treatments in 2-week-old <it>Arabidopsis </it>seedlings.</p> <p>Conclusions</p> <p>This study reports the identification of four novel ACT domain repeat proteins, ACR9 to ACR12, in <it>Arabidopsis</it>. The ACR11 and ACR12 proteins are localized to the chloroplast, and the expression of <it>ACR11 </it>and <it>GLN2 </it>is highly coordinated. These results suggest that the <it>ACR11 </it>and <it>GLN2 </it>genes may belong to the same functional module. The <it>Arabidopsis </it>ACR11 protein may function as a regulatory protein that is related to glutamine metabolism or signaling in the chloroplast.</p> http://www.biomedcentral.com/1471-2229/11/118
collection DOAJ
language English
format Article
sources DOAJ
author Hsu Chih-Ping
Chung Tsui-Yun
Sung Tzu-Ying
Hsieh Ming-Hsiun
spellingShingle Hsu Chih-Ping
Chung Tsui-Yun
Sung Tzu-Ying
Hsieh Ming-Hsiun
The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>
BMC Plant Biology
author_facet Hsu Chih-Ping
Chung Tsui-Yun
Sung Tzu-Ying
Hsieh Ming-Hsiun
author_sort Hsu Chih-Ping
title The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>
title_short The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>
title_full The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>
title_fullStr The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>
title_full_unstemmed The <it>ACR11 </it>encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with <it>GLN2 </it>in <it>Arabidopsis</it>
title_sort <it>acr11 </it>encodes a novel type of chloroplastic act domain repeat protein that is coordinately expressed with <it>gln2 </it>in <it>arabidopsis</it>
publisher BMC
series BMC Plant Biology
issn 1471-2229
publishDate 2011-08-01
description <p>Abstract</p> <p>Background</p> <p>The ACT domain, named after bacterial aspartate kinase, chorismate mutase and TyrA (prephenate dehydrogenase), is a regulatory domain that serves as an amino acid-binding site in feedback-regulated amino acid metabolic enzymes. We have previously identified a novel type of ACT domain-containing protein family, the ACT domain repeat (ACR) protein family, in <it>Arabidopsis</it>. Members of the ACR family, ACR1 to ACR8, contain four copies of the ACT domain that extend throughout the entire polypeptide. Here, we describe the identification of four novel ACT domain-containing proteins, namely ACR9 to ACR12, in <it>Arabidopsis</it>. The ACR9 and ACR10 proteins contain three copies of the ACT domain, whereas the ACR11 and ACR12 proteins have a putative transit peptide followed by two copies of the ACT domain. The functions of these plant ACR proteins are largely unknown.</p> <p>Results</p> <p>The ACR11 and ACR12 proteins are predicted to target to chloroplasts. We used protoplast transient expression assay to demonstrate that the <it>Arabidopsis </it>ACR11- and ACR12-green fluorescent fusion proteins are localized to the chloroplast. Analysis of an <it>ACR11 </it>promoter-β-glucuronidase (GUS) fusion in transgenic <it>Arabidopsis </it>revealed that the GUS activity was mainly detected in mature leaves and sepals. Interestingly, coexpression analysis revealed that the <it>GLN2</it>, which encodes a chloroplastic glutamine synthetase, has the highest mutual rank in the coexpressed gene network connected to <it>ACR11</it>. We used RNA gel blot analysis to confirm that the expression pattern of <it>ACR11 </it>is similar to that of <it>GLN2 </it>in various organs from 6-week-old <it>Arabidopsis</it>. Moreover, the expression of <it>ACR11 </it>and <it>GLN2 </it>is highly co-regulated by sucrose and light/dark treatments in 2-week-old <it>Arabidopsis </it>seedlings.</p> <p>Conclusions</p> <p>This study reports the identification of four novel ACT domain repeat proteins, ACR9 to ACR12, in <it>Arabidopsis</it>. The ACR11 and ACR12 proteins are localized to the chloroplast, and the expression of <it>ACR11 </it>and <it>GLN2 </it>is highly coordinated. These results suggest that the <it>ACR11 </it>and <it>GLN2 </it>genes may belong to the same functional module. The <it>Arabidopsis </it>ACR11 protein may function as a regulatory protein that is related to glutamine metabolism or signaling in the chloroplast.</p>
url http://www.biomedcentral.com/1471-2229/11/118
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