A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase.
Identifieur interne : 000155 ( Main/Corpus ); précédent : 000154; suivant : 000156A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase.
Auteurs : Zahra Babaei-Bondarti ; Azar ShahpiriSource :
- Phytochemistry [ 1873-3700 ] ; 2020.
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- KwdEn :
- MESH :
Abstract
Metallothioneins (MTs) are low molecular weight, cysteine-rich, metal-binding proteins that are important for essential metal homeostasis, protection against oxidative stress, and buffering against toxic heavy metals. In this work the gene encoding an MT type 2 from Avicennia marina (Forssk.) Vierh. (AmMT2) was cloned into pET41a and transformed into the Escherichia coli strain Rosetta (DE3). Following the induction with isopropyl β-D-1-thiogalactopyranoside, AmMT2 was expressed as glutathione-S-transferase (GST)-tagged fusion protein. The accumulation of Zn2+, Cu2+, Fe2+, Ni2+ and Cd2+ for strain R-AmMT2 was 4, 8, 5.4, 2 and 1.6 fold of control strain suggesting the role of AmMT2 in accumulation of metals. Particularly the strain R-AmMT2 was able to accumulate 30.7 mg per g dry weight. The cells expressing AmMT2 was more tolerant to hydrogen peroxide and had higher catalase (CAT) activity. To understand the mechanistic action of AmMT2 hydrogen peroxide tolerance, the activity of CAT in the E. coli protein extract was assayed after addition of pure Fe2+/GST-AmMT complex and Apo/GST-AmMT2 in vitro. Whereas, the activity of CAT did not change by the addition of Apo/GST-AmMT2, the activity of CAT significantly increased after addition of Fe2+/GST-AmMT2. These results show that AmMT2 activates CAT through Fe2+ transfer which subsequently causes the oxidative stress tolerance.
DOI: 10.1016/j.phytochem.2020.112396
PubMed: 32353553
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pubmed:32353553Le document en format XML
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<author><name sortKey="Babaei Bondarti, Zahra" sort="Babaei Bondarti, Zahra" uniqKey="Babaei Bondarti Z" first="Zahra" last="Babaei-Bondarti">Zahra Babaei-Bondarti</name>
<affiliation><nlm:affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan, 84156-83111, Iran.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Shahpiri, Azar" sort="Shahpiri, Azar" uniqKey="Shahpiri A" first="Azar" last="Shahpiri">Azar Shahpiri</name>
<affiliation><nlm:affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan, 84156-83111, Iran. Electronic address: a.shahpiri@iut.ac.ir.</nlm:affiliation>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase.</title>
<author><name sortKey="Babaei Bondarti, Zahra" sort="Babaei Bondarti, Zahra" uniqKey="Babaei Bondarti Z" first="Zahra" last="Babaei-Bondarti">Zahra Babaei-Bondarti</name>
<affiliation><nlm:affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan, 84156-83111, Iran.</nlm:affiliation>
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<author><name sortKey="Shahpiri, Azar" sort="Shahpiri, Azar" uniqKey="Shahpiri A" first="Azar" last="Shahpiri">Azar Shahpiri</name>
<affiliation><nlm:affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan, 84156-83111, Iran. Electronic address: a.shahpiri@iut.ac.ir.</nlm:affiliation>
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<series><title level="j">Phytochemistry</title>
<idno type="eISSN">1873-3700</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Avicennia (MeSH)</term>
<term>Catalase (MeSH)</term>
<term>Diabetes Mellitus, Type 2 (MeSH)</term>
<term>Escherichia coli (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Hydrogen Peroxide (MeSH)</term>
<term>Iron (MeSH)</term>
<term>Metallothionein (MeSH)</term>
<term>Metals, Heavy (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Catalase</term>
<term>Hydrogen Peroxide</term>
<term>Iron</term>
<term>Metallothionein</term>
<term>Metals, Heavy</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Avicennia</term>
<term>Diabetes Mellitus, Type 2</term>
<term>Escherichia coli</term>
<term>Humans</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Metallothioneins (MTs) are low molecular weight, cysteine-rich, metal-binding proteins that are important for essential metal homeostasis, protection against oxidative stress, and buffering against toxic heavy metals. In this work the gene encoding an MT type 2 from Avicennia marina (Forssk.) Vierh. (AmMT2) was cloned into pET41a and transformed into the Escherichia coli strain Rosetta (DE3). Following the induction with isopropyl β-<sub>D</sub>
-1-thiogalactopyranoside, AmMT2 was expressed as glutathione-S-transferase (GST)-tagged fusion protein. The accumulation of Zn<sup>2+</sup>
, Cu<sup>2+</sup>
, Fe<sup>2+</sup>
, Ni<sup>2+</sup>
and Cd<sup>2+</sup>
for strain R-AmMT2 was 4, 8, 5.4, 2 and 1.6 fold of control strain suggesting the role of AmMT2 in accumulation of metals. Particularly the strain R-AmMT2 was able to accumulate 30.7 mg per g dry weight. The cells expressing AmMT2 was more tolerant to hydrogen peroxide and had higher catalase (CAT) activity. To understand the mechanistic action of AmMT2 hydrogen peroxide tolerance, the activity of CAT in the E. coli protein extract was assayed after addition of pure Fe<sup>2+</sup>
/GST-AmMT complex and Apo/GST-AmMT2 in vitro. Whereas, the activity of CAT did not change by the addition of Apo/GST-AmMT2, the activity of CAT significantly increased after addition of Fe<sup>2+</sup>
/GST-AmMT2. These results show that AmMT2 activates CAT through Fe<sup>2+</sup>
transfer which subsequently causes the oxidative stress tolerance.</div>
</front>
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<Title>Phytochemistry</Title>
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<ArticleTitle>A metallothionein type 2 from Avicennia marina binds to iron and mediates hydrogen peroxide balance by activation of enzyme catalase.</ArticleTitle>
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<Abstract><AbstractText>Metallothioneins (MTs) are low molecular weight, cysteine-rich, metal-binding proteins that are important for essential metal homeostasis, protection against oxidative stress, and buffering against toxic heavy metals. In this work the gene encoding an MT type 2 from Avicennia marina (Forssk.) Vierh. (AmMT2) was cloned into pET41a and transformed into the Escherichia coli strain Rosetta (DE3). Following the induction with isopropyl β-<sub>D</sub>
-1-thiogalactopyranoside, AmMT2 was expressed as glutathione-S-transferase (GST)-tagged fusion protein. The accumulation of Zn<sup>2+</sup>
, Cu<sup>2+</sup>
, Fe<sup>2+</sup>
, Ni<sup>2+</sup>
and Cd<sup>2+</sup>
for strain R-AmMT2 was 4, 8, 5.4, 2 and 1.6 fold of control strain suggesting the role of AmMT2 in accumulation of metals. Particularly the strain R-AmMT2 was able to accumulate 30.7 mg per g dry weight. The cells expressing AmMT2 was more tolerant to hydrogen peroxide and had higher catalase (CAT) activity. To understand the mechanistic action of AmMT2 hydrogen peroxide tolerance, the activity of CAT in the E. coli protein extract was assayed after addition of pure Fe<sup>2+</sup>
/GST-AmMT complex and Apo/GST-AmMT2 in vitro. Whereas, the activity of CAT did not change by the addition of Apo/GST-AmMT2, the activity of CAT significantly increased after addition of Fe<sup>2+</sup>
/GST-AmMT2. These results show that AmMT2 activates CAT through Fe<sup>2+</sup>
transfer which subsequently causes the oxidative stress tolerance.</AbstractText>
<CopyrightInformation>Copyright © 2020 Elsevier Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Babaei-Bondarti</LastName>
<ForeName>Zahra</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan, 84156-83111, Iran.</Affiliation>
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<AffiliationInfo><Affiliation>Department of Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan, 84156-83111, Iran. Electronic address: a.shahpiri@iut.ac.ir.</Affiliation>
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<Language>eng</Language>
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<Month>04</Month>
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<MedlineJournalInfo><Country>England</Country>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>9038-94-2</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D032407" MajorTopicYN="Y">Avicennia</DescriptorName>
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<MeshHeading><DescriptorName UI="D002374" MajorTopicYN="N">Catalase</DescriptorName>
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<MeshHeading><DescriptorName UI="D003924" MajorTopicYN="Y">Diabetes Mellitus, Type 2</DescriptorName>
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<MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName>
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<MeshHeading><DescriptorName UI="D008668" MajorTopicYN="N">Metallothionein</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019216" MajorTopicYN="Y">Metals, Heavy</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Acanthaceae</Keyword>
<Keyword MajorTopicYN="N">Avicennia marina</Keyword>
<Keyword MajorTopicYN="N">Hydrogen peroxide tolerance</Keyword>
<Keyword MajorTopicYN="N">Iron</Keyword>
<Keyword MajorTopicYN="N">Metal accumulation</Keyword>
<Keyword MajorTopicYN="N">Metallothionein</Keyword>
<Keyword MajorTopicYN="N">Recombinant protein</Keyword>
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