Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor
<strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaver...
Ausführliche Beschreibung
Autor*in: |
Zahra Soleimani [verfasserIn] Sedigheh Fabriki [verfasserIn] Soodabeh Mafakheri [verfasserIn] |
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E-Artikel |
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Sprache: |
Persisch |
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2018 |
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Übergeordnetes Werk: |
In: مجله بیوتکنولوژی کشاورزی - Shahid Bahonar University of Kerman, 2020, 10(2018), 2, Seite 94-107 |
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Übergeordnetes Werk: |
volume:10 ; year:2018 ; number:2 ; pages:94-107 |
Links: |
Link aufrufen |
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DOI / URN: |
10.22103/jab.2018.2153 |
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Katalog-ID: |
DOAJ002174669 |
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520 | |a <strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. | ||
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10.22103/jab.2018.2153 doi (DE-627)DOAJ002174669 (DE-599)DOAJ3208e43f68b548eba839b35b242b7dee DE-627 ger DE-627 rakwb per TP248.13-248.65 Zahra Soleimani verfasserin aut Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. benzylisoquinoline celandine cmmsh salinity sanguinarine Agriculture S Biotechnology Sedigheh Fabriki verfasserin aut Soodabeh Mafakheri verfasserin aut In مجله بیوتکنولوژی کشاورزی Shahid Bahonar University of Kerman, 2020 10(2018), 2, Seite 94-107 (DE-627)1699004935 22286500 nnns volume:10 year:2018 number:2 pages:94-107 https://doi.org/10.22103/jab.2018.2153 kostenfrei https://doaj.org/article/3208e43f68b548eba839b35b242b7dee kostenfrei https://jab.uk.ac.ir/article_2153_5e529a1e9634a1d82f6e4ef726603ef4.pdf kostenfrei https://doaj.org/toc/2228-6705 Journal toc kostenfrei https://doaj.org/toc/2228-6500 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 10 2018 2 94-107 |
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10.22103/jab.2018.2153 doi (DE-627)DOAJ002174669 (DE-599)DOAJ3208e43f68b548eba839b35b242b7dee DE-627 ger DE-627 rakwb per TP248.13-248.65 Zahra Soleimani verfasserin aut Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. benzylisoquinoline celandine cmmsh salinity sanguinarine Agriculture S Biotechnology Sedigheh Fabriki verfasserin aut Soodabeh Mafakheri verfasserin aut In مجله بیوتکنولوژی کشاورزی Shahid Bahonar University of Kerman, 2020 10(2018), 2, Seite 94-107 (DE-627)1699004935 22286500 nnns volume:10 year:2018 number:2 pages:94-107 https://doi.org/10.22103/jab.2018.2153 kostenfrei https://doaj.org/article/3208e43f68b548eba839b35b242b7dee kostenfrei https://jab.uk.ac.ir/article_2153_5e529a1e9634a1d82f6e4ef726603ef4.pdf kostenfrei https://doaj.org/toc/2228-6705 Journal toc kostenfrei https://doaj.org/toc/2228-6500 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 10 2018 2 94-107 |
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10.22103/jab.2018.2153 doi (DE-627)DOAJ002174669 (DE-599)DOAJ3208e43f68b548eba839b35b242b7dee DE-627 ger DE-627 rakwb per TP248.13-248.65 Zahra Soleimani verfasserin aut Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. benzylisoquinoline celandine cmmsh salinity sanguinarine Agriculture S Biotechnology Sedigheh Fabriki verfasserin aut Soodabeh Mafakheri verfasserin aut In مجله بیوتکنولوژی کشاورزی Shahid Bahonar University of Kerman, 2020 10(2018), 2, Seite 94-107 (DE-627)1699004935 22286500 nnns volume:10 year:2018 number:2 pages:94-107 https://doi.org/10.22103/jab.2018.2153 kostenfrei https://doaj.org/article/3208e43f68b548eba839b35b242b7dee kostenfrei https://jab.uk.ac.ir/article_2153_5e529a1e9634a1d82f6e4ef726603ef4.pdf kostenfrei https://doaj.org/toc/2228-6705 Journal toc kostenfrei https://doaj.org/toc/2228-6500 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 10 2018 2 94-107 |
allfieldsGer |
10.22103/jab.2018.2153 doi (DE-627)DOAJ002174669 (DE-599)DOAJ3208e43f68b548eba839b35b242b7dee DE-627 ger DE-627 rakwb per TP248.13-248.65 Zahra Soleimani verfasserin aut Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. benzylisoquinoline celandine cmmsh salinity sanguinarine Agriculture S Biotechnology Sedigheh Fabriki verfasserin aut Soodabeh Mafakheri verfasserin aut In مجله بیوتکنولوژی کشاورزی Shahid Bahonar University of Kerman, 2020 10(2018), 2, Seite 94-107 (DE-627)1699004935 22286500 nnns volume:10 year:2018 number:2 pages:94-107 https://doi.org/10.22103/jab.2018.2153 kostenfrei https://doaj.org/article/3208e43f68b548eba839b35b242b7dee kostenfrei https://jab.uk.ac.ir/article_2153_5e529a1e9634a1d82f6e4ef726603ef4.pdf kostenfrei https://doaj.org/toc/2228-6705 Journal toc kostenfrei https://doaj.org/toc/2228-6500 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 10 2018 2 94-107 |
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TP248.13-248.65 Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor benzylisoquinoline celandine cmmsh salinity sanguinarine |
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Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor |
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<strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. |
abstractGer |
<strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. |
abstract_unstemmed |
<strong< </strong< The greater celandine (<em<Chelidonium majus</em< L.) contains important alkaloids such as Sanguinarine. Sanguinarine is an active alkaloid with potentially antimicrobial, anti-inflammatory and anti-tumor properties that is widely found in plants of Papaveraceae family. In this research, the isolation and sequencing of (s)-cis-N-methyl stylopine 14-hydroxylas (MSH) coding gene was performed as one of the key enzymes in Sanguinarine pathway from celandine. Then, the changes in <em<cmMSH</em< gene expression were investigated in roots, leave and stems at four salinity levels (0, 25, 50, and 100 mM) in a factorial experiment based on completely randomized design. In the present study, the cDNA encoding MSH enzyme was isolated from root and successfully integrated into PTG19-T plasmid and cloned at E. coli. After confirmation of recombinant clones by PCR, plasmids of recombinant bacteria were extracted and the gene segment sequenced. The sequenced segment had 784 nucleotides with an open reading frame of 261 amino acids which the derived protein with functional domains including helix K region, heme-binding region and aromatic region belonged to the Cytochrome-P450 protein family. In the phylogeny tree, the protein sequence of isolated <em<cmMSH</em< gene had the most similarity with methylstylopine 14-hydroxylase enzyme of poppy species. Mean comparison of gene relative expression showed that 50 mM salinity had maximal effect on increasing of <em<cmMSH</em< gene expression in root tissue. Also, the expression pattern showed that with increment the salinity up to 50 mM, the expression of <em<cmMSH</em< gene increased in leaves and roots, but with increment the salinity to 100 mM the gene expression decreased 35% in both tissues. |
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title_short |
Molecular isolation of cDNA encoding N-methylstylopine hydroxylase from greater celandine (Chelidonium majus L.) and its expression enhancement in response to salinity abiotic elicitor |
url |
https://doi.org/10.22103/jab.2018.2153 https://doaj.org/article/3208e43f68b548eba839b35b242b7dee https://jab.uk.ac.ir/article_2153_5e529a1e9634a1d82f6e4ef726603ef4.pdf https://doaj.org/toc/2228-6705 https://doaj.org/toc/2228-6500 |
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Sedigheh Fabriki Soodabeh Mafakheri |
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