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Recovery of heat shock-triggered released apoplastic Ca2 accompanied by pectin methylesterase activity is required for thermotolerance in soybean seedlings

Identifieur interne : 001499 ( Istex/Corpus ); précédent : 001498; suivant : 001500

Recovery of heat shock-triggered released apoplastic Ca2 accompanied by pectin methylesterase activity is required for thermotolerance in soybean seedlings

Auteurs : Hui-Chen Wu ; Shih-Feng Hsu ; Dan-Li Luo ; Shiang-Jiuun Chen ; Wen-Dar Huang ; Huu-Sheng Lur ; Tsung-Luo Jinn

Source :

RBID : ISTEX:B803D941E5DBFB3FA8BB3B2360C33FF9AA806EE0

Abstract

Synthesis of heat shock proteins (HSPs) in response to heat shock (HS) is essential for thermotolerance. The effect of a Ca2 chelator, EGTA, was investigated before a lethal HS treatment in soybean (Glycine max) seedlings with acquired thermotolerance induced by preheating. Such seedlings became non-thermotolerant with EGTA treatment. The addition of Ca2, Sr2 or Ba2 to the EGTA-treated samples rescued the seedlings from death by preventing the increased cellular leakage of electrolytes, amino acids, and sugars caused by EGTA. It was confirmed that EGTA did not affect HSP accumulation and physiological functions but interfered with the recovery of HS-released Ca2 concentration which was required for thermotolerance. Pectin methylesterase (PME, EC 3.1.1.11), a cell wall remodelling enzyme, was activated in response to HS, and its elevated activity caused an increased level of demethylesterified pectin which was related to the recovery of the HS-released Ca2 concentration. Thus, the recovery of HS-released Ca2 in Ca2-pectate reconstitution through PME activity is required for cell wall remodelling during HS in soybean which, in turn, retains plasma membrane integrity and co-ordinates with HSPs to confer thermotolerance.

Url:
DOI: 10.1093/jxb/erq121

Links to Exploration step

ISTEX:B803D941E5DBFB3FA8BB3B2360C33FF9AA806EE0

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<aff id="aff1">
<label>1</label>
Institute of Plant Biology and Department of Life Science, National Taiwan University, Taipei 10617, Taiwan</aff>
<aff id="aff2">
<label>2</label>
Department of Agronomy, National Taiwan University, Taipei 10617, Taiwan</aff>
<author-notes>
<corresp id="cor1">
<label>*</label>
To whom correspondence should be addressed: E-mail:
<email>jinnt@ntu.edu.tw</email>
</corresp>
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<pub-date pub-type="ppub">
<month>06</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="epub">
<day>05</day>
<month>05</month>
<year>2010</year>
</pub-date>
<volume>61</volume>
<issue>10</issue>
<fpage>2843</fpage>
<lpage>2852</lpage>
<history>
<date date-type="received">
<day>20</day>
<month>1</month>
<year>2010</year>
</date>
<date date-type="rev-recd">
<day>9</day>
<month>4</month>
<year>2010</year>
</date>
<date date-type="accepted">
<day>12</day>
<month>4</month>
<year>2010</year>
</date>
</history>
<permissions>
<copyright-statement>© 2010 The Author(s).</copyright-statement>
<copyright-year>2010</copyright-year>
<license license-type="open-access">
<p>This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.</p>
<p>This paper is available online free of all access charges (see
<ext-link ext-link-type="uri" xlink:href="http://jxb.oxfordjournals.org/open_access.html">http://jxb.oxfordjournals.org/open_access.html</ext-link>
for further details)</p>
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<abstract>
<p>Synthesis of heat shock proteins (HSPs) in response to heat shock (HS) is essential for thermotolerance. The effect of a Ca
<sup>2+</sup>
chelator, EGTA, was investigated before a lethal HS treatment in soybean (
<italic>Glycine max</italic>
) seedlings with acquired thermotolerance induced by preheating. Such seedlings became non-thermotolerant with EGTA treatment. The addition of Ca
<sup>2+</sup>
, Sr
<sup>2+</sup>
or Ba
<sup>2+</sup>
to the EGTA-treated samples rescued the seedlings from death by preventing the increased cellular leakage of electrolytes, amino acids, and sugars caused by EGTA. It was confirmed that EGTA did not affect HSP accumulation and physiological functions but interfered with the recovery of HS-released Ca
<sup>2+</sup>
concentration which was required for thermotolerance. Pectin methylesterase (PME, EC 3.1.1.11), a cell wall remodelling enzyme, was activated in response to HS, and its elevated activity caused an increased level of demethylesterified pectin which was related to the recovery of the HS-released Ca
<sup>2+</sup>
concentration. Thus, the recovery of HS-released Ca
<sup>2+</sup>
in Ca
<sup>2+</sup>
-pectate reconstitution through PME activity is required for cell wall remodelling during HS in soybean which, in turn, retains plasma membrane integrity and co-ordinates with HSPs to confer thermotolerance.</p>
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<abstract>Synthesis of heat shock proteins (HSPs) in response to heat shock (HS) is essential for thermotolerance. The effect of a Ca2 chelator, EGTA, was investigated before a lethal HS treatment in soybean (Glycine max) seedlings with acquired thermotolerance induced by preheating. Such seedlings became non-thermotolerant with EGTA treatment. The addition of Ca2, Sr2 or Ba2 to the EGTA-treated samples rescued the seedlings from death by preventing the increased cellular leakage of electrolytes, amino acids, and sugars caused by EGTA. It was confirmed that EGTA did not affect HSP accumulation and physiological functions but interfered with the recovery of HS-released Ca2 concentration which was required for thermotolerance. Pectin methylesterase (PME, EC 3.1.1.11), a cell wall remodelling enzyme, was activated in response to HS, and its elevated activity caused an increased level of demethylesterified pectin which was related to the recovery of the HS-released Ca2 concentration. Thus, the recovery of HS-released Ca2 in Ca2-pectate reconstitution through PME activity is required for cell wall remodelling during HS in soybean which, in turn, retains plasma membrane integrity and co-ordinates with HSPs to confer thermotolerance.</abstract>
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