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a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
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a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
additional information
?
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a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin + 2 H2O
(9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid] i.e. linoleoyl-[glycerolipid]
(9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid] i.e. alpha-linolenoyl-[glycerolipid]
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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-
?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
additional information
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enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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additional information
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enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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additional information
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enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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additional information
?
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enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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additional information
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FAD7 utilizes ferredoxin as the intermediate electron donor to act upon fatty acids esterified to galactolipids, sulfolipid, and phosphatidylglycerol
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additional information
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FAD7 utilizes ferredoxin as the intermediate electron donor to act upon fatty acids esterified to galactolipids, sulfolipid, and phosphatidylglycerol
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additional information
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FAD7 utilizes ferredoxin as the intermediate electron donor to act upon fatty acids esterified to galactolipids, sulfolipid, and phosphatidylglycerol
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a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
additional information
?
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a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
an alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
alpha-linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
alpha-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
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?
additional information
?
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enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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?
additional information
?
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enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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?
additional information
?
-
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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?
additional information
?
-
enzyme FAD8 has a higher selectivity for 18:2 acyl-lipid substrates and a higher preference for lipids other than galactolipids, particularly phosphatidylglycerol, at any of the temperatures studied
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?
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developing
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enzyme levels increase during growth and maturation at 15-26°C
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enzyme levels increase during growth and maturation at 15-26°C
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young
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gene fad7 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
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gene fad8 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
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gene fad7 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
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gene fad8 is expressed in leaves, but not in roots at normal temperature- and low temperature-growth conditions
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low expression level
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induction at high salt condition
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induction at high salt condition
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additional information
tissue-specific expression
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additional information
tissue-specific expression
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additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD7 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
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additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD7 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
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additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD8 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
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additional information
tissue-specific analysis of fatty acid patterns, overview. Enzyme FAD8 is detected in all vegetative tissues, and more abundant in the shoots and mature leaves, which are rich in chlorophyll, expression patterns
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additional information
no or little expression is detected in mature seeds, roots and stems
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additional information
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tissue-specific expression
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additional information
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FAD7-1 is normally expressed in tissues apart from roots and developing seeds. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
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additional information
FAD7-1 is normally expressed in tissues apart from roots and developing seeds. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
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additional information
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FAD7-2 is highly expressed in leaves and roots. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
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additional information
FAD7-2 is highly expressed in leaves and roots. PfrFAD7-1 and PfrFAD7-2 genes are expressed at low levels during all stages of developing seeds as compared with expression levels in leaves
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additional information
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tissue-specific expression
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additional information
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tissue-specific expression
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additional information
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tissue-specific expression
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additional information
tissue-specific expression
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additional information
the overall level of ZmFAD7 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD7 is dominantly expressed at 25°C, moderate expression at 15°C, no expression at 5°C
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additional information
the overall level of ZmFAD7 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD7 is dominantly expressed at 25°C, moderate expression at 15°C, no expression at 5°C
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additional information
the overall level of ZmFAD8 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD8 is dominantly expressed at 5°C, moderate expression at 15°C, no expression at 25°C
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additional information
the overall level of ZmFAD8 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD8 is dominantly expressed at 5°C, moderate expression at 15°C, no expression at 25°C
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additional information
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the overall level of ZmFAD7 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD7 is dominantly expressed at 25°C, moderate expression at 15°C, no expression at 5°C
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additional information
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the overall level of ZmFAD8 transcript is increased after exposure to 5°C but not above 10°C. ZmFAD8 is dominantly expressed at 5°C, moderate expression at 15°C, no expression at 25°C
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evolution
three histidine clusters characteristic of fatty acid desaturases, a putative chloroplast transit peptide in the N-terminal, and three putative transmembrane domains are identified in the enzyme sequence
metabolism
glycine betaine protects tomato plants at low temperature by inducing fatty acid desaturase7 and lipoxygenase gene expression, providing protection against cold stress in tomato plants which might be related to the desaturation process of lipids leading to increased membrane stability and/or induction of other genes related to stress defense mechanisms via octadecanoid pathway or lipid peroxidation products
malfunction
in a genetic background that is wild type at the FAD7 locus, the fad8 mutation has no detedable effed on overall leaf fatty acid composition irrespective of the temperature at which plants are grown. However, fatty acid analyses of individual leaf lipids reveales small decreases in the levels of 18:3 in two chloroplast lipids. In fad8 plants grown at 22°C, phosphatidylglycerol contains 22.5% 18:3 compared with 33.5% in wild type Arabidopsis
malfunction
mutations at the fad7 locus of Arabidopsis thaliana cause decreased desaturation of dienoic fatty acids in chloroplast lipids in plants grown at elevated temperatures
malfunction
mutations at the fad7 locus of Arabidopsis thaliana cause decreased desaturation of dienoic fatty acids in chloroplast lipids in plants grown at elevated temperatures
malfunction
a fad8 mutant shows no significant changes in its fatty acid profile at a control (22°C) temperature, while at lower temperature (15°C) the mutant shows a phenotype, leaf lipid analysis, overview
malfunction
comparison of trienoic fatty acid levels in wild-type and fad7 mutant leaves, an increase occurs in the wild-type at 15-26°C during maturation mainly due to galactolipids enriched in plastid membranes, while in mutant leaves at 26°C the levels decrease with leaf maturation, overview
malfunction
in contrast to avirulent petiole exudates from wild-type plants, avirulent petiole exudates from fad7, sfd1 and sfd2 mutants are unable to activate systemic acquired resistance when applied to wild-type plants. The SAR-inducing activity is reconstituted by mixing avirulent petiole exudates collected from fad7 and sfd1 with avirulent petiole exudate from the SAR-deficient dir1 mutant
malfunction
mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable. After disruption of the AtFAD7 gene, enzyme FAD8 enzymatic activity is able to maintain, at least partially (43.7%), the amount of 18:3 and to a much lesser extent that of 16:3 (23.2%) at 22°C
malfunction
the omega-3 fatty acids hexadecatrienoic acid (C16:3n3), hexadecatetraenoic acid (C16:4),and alpha-linolenic acid (C18:3n3) are not detected in the CC-620 strain, phenotype and fatty acid composition of the omega-3 fatty acid deficiency in strain CC-620 due to the missense mutation detected in gene CrFAD7, complementation by the wild-type enzyme, overview
malfunction
leaf lipid analysis of the Arabidopsis omega-3 desaturase fad7 mutant line at growth temperature of 22°C, overview. Disruption of the AtFAD7 gene in fad7i mutant results in a reduction of TAs with an 18:3 content of 29.6% and an even more reduced content of 16:3 down to 2%. Mutant fad7i maintains 74% of 18:3 production with respect to wild-type Col-0 while only 23% of 16:3 synthesis is maintained in the mutant
malfunction
osfad8 knockout mutant plants exhibit significant alterations in fatty acid unsaturation for all four investigated plastidic lipid classes. During a 5-day acclimation period at 4°C, further changes in fatty acid unsaturation in both wild-type and mutant plants vary according to the type of lipid. The fluidity of the thylakoid membrane are altered significantly by both FAD8 mutation and cold acclimation, suggesting that factors other than FAD8 are involved in C18 fatty acid unsaturation and fluctuations in membrane fluidity. Similarly, significant changes are noted for both the mutant and wild-type samples in terms of their fatty acid compositions as well as activities related to photosystem (PS) I, PSII, and photoprotection. This includes the development of non-photochemical quenching and increased zeaxanthin accumulation. Despite the relatively small changes in fatty acid composition during cold acclimation, cold-inducible FAD8 knock-out mutants display strong differences in photoprotective activities and a further drop in membrane fluidity. The mutants are more sensitive than wild-type to short-term low-temperature stress that results in increased production of reactive oxygen species after 5 days of chilling. The levels of 18:3 are reduced by 20% in the fad8 knockout mutant compared to wild-type, while the levels of 18:2 are increased 2fold. Phenotype, overview
malfunction
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leaf lipid analysis of the Arabidopsis omega-3 desaturase fad7 mutant line at growth temperature of 22°C, overview. Disruption of the AtFAD7 gene in fad7i mutant results in a reduction of TAs with an 18:3 content of 29.6% and an even more reduced content of 16:3 down to 2%. Mutant fad7i maintains 74% of 18:3 production with respect to wild-type Col-0 while only 23% of 16:3 synthesis is maintained in the mutant
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malfunction
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mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable. After disruption of the AtFAD7 gene, enzyme FAD8 enzymatic activity is able to maintain, at least partially (43.7%), the amount of 18:3 and to a much lesser extent that of 16:3 (23.2%) at 22°C
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malfunction
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comparison of trienoic fatty acid levels in wild-type and fad7 mutant leaves, an increase occurs in the wild-type at 15-26°C during maturation mainly due to galactolipids enriched in plastid membranes, while in mutant leaves at 26°C the levels decrease with leaf maturation, overview
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malfunction
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a fad8 mutant shows no significant changes in its fatty acid profile at a control (22°C) temperature, while at lower temperature (15°C) the mutant shows a phenotype, leaf lipid analysis, overview
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physiological function
FAD7-synthesized lipids provide fatty acids for synthesis of jasmonic acid. Petiole exudates collected from Arabidopsis leaves inoculated with an avirulent Pseudomonas syringae strain promote systemic acquired resistance, SAR, when applied to Arabidopsis thaliana. Arabidopsis fatty acid desaturase7, suppressor of fatty acid desaturase deficiency 1 (SFD1), and SFD2 genes are required for accumulation of the SAR-inducing activity. Jasmonic acid and methyljasmonic acid with avirulent petiole exudate from fad7 and sfd1 does not reconstitute the SAR-inducing activity. A plastid glycerolipid-dependent factor is required in avirulent petiole exudate along with the DIR1-encoded lipid transfer protein for long-distance signaling in systemic acquired resistance
physiological function
fatty acid desaturases catalyze the introduction of double bonds into the aliphatic tails of fatty acids which affects plant responses against a variety of stresses via the enhancement of membrane fluidity
physiological function
plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C
physiological function
plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C, indicating that enzyme FAD8 is active at this growth temperature, contrasting to previous observations that circumscribe the FAD8 activity at low temperatures
physiological function
role of omega-3 fatty acid desaturases in the positive regulation of the level of trienoic fatty acids during leaf cell maturation
physiological function
the plastidial omega-3 fatty acid desaturase FAD7 catalyzes the desaturation of dienoic fatty acids in membrane lipids
physiological function
the role of fad8 is to provide increased omega3 desaturase activity in plants that are exposed to low growth temperature
physiological function
Thr residue located in the fourth transmembrane domain of fatty acid desaturase 7 (FAD7) that is essential for the biosynthesis of omega-3 fatty acids in Chlamydomonas reinhardtii, Thr286 is essential for the maintaining the catalytic structure of the enzyme
physiological function
plastidial omega-3 desaturase FAD7 is a major contributor to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Differences in the mechanism controlling AtFAD7 and AtFAD8 gene expression at different temperatures, the function of both plastidial omega-3 desaturases is coordinated in a non-redundant manner
physiological function
the plastidial omega-3-fatty acid desaturases CsFAD7 and CsFAD8 are both responsive to abiotic stress signals, but they may play very different roles during stress tolerance in tea plants
physiological function
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plastidial omega-3 desaturase FAD7 is a major contributor to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Differences in the mechanism controlling AtFAD7 and AtFAD8 gene expression at different temperatures, the function of both plastidial omega-3 desaturases is coordinated in a non-redundant manner
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physiological function
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plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C
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physiological function
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the plastidial omega-3 fatty acid desaturase FAD7 catalyzes the desaturation of dienoic fatty acids in membrane lipids
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physiological function
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role of omega-3 fatty acid desaturases in the positive regulation of the level of trienoic fatty acids during leaf cell maturation
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physiological function
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plastidial omega-3 desaturases FAD7 and FAD8 are major contributors to trienoic fatty acid biosynthesis in the leaves of Arabidopsis thaliana plants. Enzyme FAD8 partially compensates the disruption of the AtFAD7 gene at 22°C, indicating that enzyme FAD8 is active at this growth temperature, contrasting to previous observations that circumscribe the FAD8 activity at low temperatures
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physiological function
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the role of fad8 is to provide increased omega3 desaturase activity in plants that are exposed to low growth temperature
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additional information
ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids. Overexpression of FAD8 leads to increased tolerance to osmotic stress (imposed by two different agents, PEG 8000 and sorbitol) and decreased tolerance to heat stress (35°C), at both cellular and whole-plant levels. FAD8-overexpressing plants can regain growth after withholding water for a duration that severely impaires the ability of wild-type plants to recover from the stress. Fatty acid composition of leaf polar lipids of wild-type and transgenic plants, overview
additional information
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity, the C-terminal region of FAD8 desaturase is essential for destabilization at high temperature (22°C). The C-terminal coding region of FAD8 is sufficient to suppress the accumulation of plastidial omega-3 desaturase protein at high temperature, overview
additional information
elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity, the C-terminal region of FAD8 desaturase is essential for destabilization at high temperature (22°C). The C-terminal coding region of FAD8 is sufficient to suppress the accumulation of plastidial omega-3 desaturase protein at high temperature, overview
additional information
FAD8-YFP over-expressing lines show a specific increase in 18:3 fatty acids at 22°C. Residue 103 is part of the first His box essential for desaturase function
additional information
FAD8-YFP over-expressing lines show a specific increase in 18:3 fatty acids at 22°C. Residue 103 is part of the first His box essential for desaturase function
additional information
increased levels of trienoic fatty acids in genetically engineered plants enhance cold tolerance
additional information
wounding changes the spatial expression pattern of the FAD7 gene
additional information
fatty acids contents (mol%) in leaves from wild-type rice and osfad8 mutant lines at 4°C and 28°C, overview. Membrane fluidity of rice plants is altered with altered fatty acid compositions
additional information
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wounding changes the spatial expression pattern of the FAD7 gene
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additional information
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increased levels of trienoic fatty acids in genetically engineered plants enhance cold tolerance
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additional information
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elevated temperatures lead to decreases in leaf trienoic fatty acid level due to temperature sensitivity of enzyme FAD8 activity, the C-terminal region of FAD8 desaturase is essential for destabilization at high temperature (22°C). The C-terminal coding region of FAD8 is sufficient to suppress the accumulation of plastidial omega-3 desaturase protein at high temperature, overview
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additional information
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FAD8-YFP over-expressing lines show a specific increase in 18:3 fatty acids at 22°C. Residue 103 is part of the first His box essential for desaturase function
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additional information
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ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids. Overexpression of FAD8 leads to increased tolerance to osmotic stress (imposed by two different agents, PEG 8000 and sorbitol) and decreased tolerance to heat stress (35°C), at both cellular and whole-plant levels. FAD8-overexpressing plants can regain growth after withholding water for a duration that severely impaires the ability of wild-type plants to recover from the stress. Fatty acid composition of leaf polar lipids of wild-type and transgenic plants, overview
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C103Y
mutation occuring in the fad3 fad7 fad8 triple mutant
W149stop
the fads-1 mutation creates a premature stop codon 149 amino acids from the N-terminal end of the fad8 open reading frame, the mutation results in a complete loss of fad8 activity
C103Y
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mutation occuring in the fad3 fad7 fad8 triple mutant
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W149stop
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the fads-1 mutation creates a premature stop codon 149 amino acids from the N-terminal end of the fad8 open reading frame, the mutation results in a complete loss of fad8 activity
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T286C
site-directed mutagenesis, omega3-fatty acid deficiency mutant
T286G
site-directed mutagenesis, omega3-fatty acid deficiency mutant
T286H
site-directed mutagenesis, omega3-fatty acid deficiency mutant
T286N
naturally occuring mutation causing omega3-fatty acid deficiency in strain CC-620, that can be recovered by overexpression of the wild-type enzyme from strain CC-125
T286S
site-directed mutagenesis, the mutant shows partially reduced enzyme activity
T286Y
site-directed mutagenesis, omega3-fatty acid deficiency mutant
additional information
constitutive expression of the fad8 cDNA in transgenic plants of a fad7 mutant JBl01, via Agrobacterium turnefaciens C58 (pGV3101) containing plasmid pBI/fad8 or pBIl2l, results in genetic complementation of the mutation, indicating that the fad7 and fad8 gene products are functionally equivalent. Expression of the fad8 cDNA in transgenic plants often results in the co-suppression of both the endogenous fad7 and fad8 genes in spite of the fact that these two genes share only about 75% nucleotide identity
additional information
constitutive expression of the fad8 cDNA in transgenic plants of a fad7 mutant JBl01, via Agrobacterium turnefaciens C58 (pGV3101) containing plasmid pBI/fad8 or pBIl2l, results in genetic complementation of the mutation, indicating that the fad7 and fad8 gene products are functionally equivalent. Expression of the fad8 cDNA in transgenic plants often results in the co-suppression of both the endogenous fad7 and fad8 genes in spite of the fact that these two genes share only about 75% nucleotide identity
additional information
construction of a fad7/fad8 double mutant with reduced overall levels of trienoic fatty acids in leaf tissues. A series of FAD7-FAD8 chimeric genes, each encoding a functional plastidial omega-3 desaturase, are introduced into the Arabidopsis thaliana fad7/fad8 double mutant, structures, overview. All transformants show an unaltered temperature response, and none of the transformants exhibit an exceptional phenotype
additional information
construction of a fad7/fad8 double mutant with reduced overall levels of trienoic fatty acids in leaf tissues. A series of FAD7-FAD8 chimeric genes, each encoding a functional plastidial omega-3 desaturase, are introduced into the Arabidopsis thaliana fad7/fad8 double mutant, structures, overview. All transformants show an unaltered temperature response, and none of the transformants exhibit an exceptional phenotype
additional information
construction of a tandem T-DNA FAD7 insertion omega-3 desaturase mutant line SALK_147096C/fad7i. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
additional information
construction of a tandem T-DNA FAD7 insertion omega-3 desaturase mutant line SALK_147096C/fad7i. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
additional information
construction of a tandem T-DNA FAD8 insertion omega-3 desaturase mutant line SALK_093590 with no phenotype at 22°C. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. FAD8-YFP overexpressing lines show a specific increase in 18:3 fatty acids at 22°C. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Disruption of the AtFAD8 gene in mutant fad8i results in trienoic fatty acid levels almost similar to those from wild-type Col-0. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
additional information
construction of a tandem T-DNA FAD8 insertion omega-3 desaturase mutant line SALK_093590 with no phenotype at 22°C. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. FAD8-YFP overexpressing lines show a specific increase in 18:3 fatty acids at 22°C. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Disruption of the AtFAD8 gene in mutant fad8i results in trienoic fatty acid levels almost similar to those from wild-type Col-0. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
additional information
generation of the fad7 knockout mutant line JB101
additional information
recombinant overexpression of FAD8 increases tolerance to drought in tobacco plants and to osmotic stress in cultured cells. Ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids
additional information
the fad7-1 mutant JB101 is deficient of plastid omega-3 desaturase FAD7 enzyme activity, the defect is due to mRNA destabilization, not deregulation
additional information
construction of a insertional mutant fad7i (SALK_147096C) inactivation mutant of FAD7, analysis of the fatty acid composition of the fad7i mutant shows compensatory responses at the TA level as a result of inactivation of the FAD7 gene, absence of AtFAD7 transcript in the mutant. Contruction of a fad7/fad8 double knockout mutant. Given the strong reduction (70%) in 18:3 content observed in the fad7/fad8 double mutant, in mutant fad7i after disruption of the AtFAD7 gene, FAD8 enzymatic activity is able to maintain, at least partially (43.7%), the amount of 18:3 and to a much lesser extent that of 16:3 (23.2%) at 22°C. Mutant genotypes and phenotypes, overview. Temperature-dependent expression levels. Disruption of the AtFAD7 gene in the insertion mutant does not result in significant changes in the transcript levels of FAD7
additional information
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construction of a insertional mutant fad7i (SALK_147096C) inactivation mutant of FAD7, analysis of the fatty acid composition of the fad7i mutant shows compensatory responses at the TA level as a result of inactivation of the FAD7 gene, absence of AtFAD7 transcript in the mutant. Contruction of a fad7/fad8 double knockout mutant. Given the strong reduction (70%) in 18:3 content observed in the fad7/fad8 double mutant, in mutant fad7i after disruption of the AtFAD7 gene, FAD8 enzymatic activity is able to maintain, at least partially (43.7%), the amount of 18:3 and to a much lesser extent that of 16:3 (23.2%) at 22°C. Mutant genotypes and phenotypes, overview. Temperature-dependent expression levels. Disruption of the AtFAD7 gene in the insertion mutant does not result in significant changes in the transcript levels of FAD7
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additional information
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construction of a fad7/fad8 double mutant with reduced overall levels of trienoic fatty acids in leaf tissues. A series of FAD7-FAD8 chimeric genes, each encoding a functional plastidial omega-3 desaturase, are introduced into the Arabidopsis thaliana fad7/fad8 double mutant, structures, overview. All transformants show an unaltered temperature response, and none of the transformants exhibit an exceptional phenotype
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additional information
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the fad7-1 mutant JB101 is deficient of plastid omega-3 desaturase FAD7 enzyme activity, the defect is due to mRNA destabilization, not deregulation
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additional information
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construction of a tandem T-DNA FAD7 insertion omega-3 desaturase mutant line SALK_147096C/fad7i. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Mutant fad7i maintains 74% of 18:3 production with respect to Col-0 while only 23% of 16:3 synthesis is maintained in this mutant. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
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additional information
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constitutive expression of the fad8 cDNA in transgenic plants of a fad7 mutant JBl01, via Agrobacterium turnefaciens C58 (pGV3101) containing plasmid pBI/fad8 or pBIl2l, results in genetic complementation of the mutation, indicating that the fad7 and fad8 gene products are functionally equivalent. Expression of the fad8 cDNA in transgenic plants often results in the co-suppression of both the endogenous fad7 and fad8 genes in spite of the fact that these two genes share only about 75% nucleotide identity
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additional information
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generation of the fad7 knockout mutant line JB101
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additional information
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construction of a tandem T-DNA FAD8 insertion omega-3 desaturase mutant line SALK_093590 with no phenotype at 22°C. Construction of double fad7/fad8 and triple fad3/fad7/fad8 mutants. FAD8-YFP overexpressing lines show a specific increase in 18:3 fatty acids at 22°C. Fatty acid composition of total leaf lipids from wild-type and the different mutant lines grown at 22°C, overview. Disruption of the AtFAD8 gene in mutant fad8i results in trienoic fatty acid levels almost similar to those from wild-type Col-0. The fad7/fad8 double mutant also shows a considerable reduction in trienoic fatty acids, particularly in 16:3, which is undetectable
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additional information
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recombinant overexpression of FAD8 increases tolerance to drought in tobacco plants and to osmotic stress in cultured cells. Ectopic overexpression of FAD8 induces an increased ratio mainly in the plastidic lipids
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additional information
mutation of Thr286 may directly affect the structure of the transmembrane domain of the enzyme
additional information
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mutation of Thr286 may directly affect the structure of the transmembrane domain of the enzyme
additional information
the removal of the plastidial transit peptide and the incorporation of a KKNL motif to the C-terminus of HaFAD7 increases the activity by 10fold compared to the native protein. N-terminal fusion of transmembrane-domains from either the Saccharomyces cerevisiae microsomal ELO3, (a type III signal anchor domain), or FAE1, an endoplasmic reticulum membrane anchoring domain, results in moderate increases in enzyme activity. Fusing a hemagglutinin epitope tag upstream of an endogenous C-terminal KEK motif results in a significant loss of activity compared to the un-tagged construct, indicating that the endogenous KEK C-terminal di-lysine motif is capable of directing in yeast the ER-retention of this normally plastidial-located protein
additional information
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the removal of the plastidial transit peptide and the incorporation of a KKNL motif to the C-terminus of HaFAD7 increases the activity by 10fold compared to the native protein. N-terminal fusion of transmembrane-domains from either the Saccharomyces cerevisiae microsomal ELO3, (a type III signal anchor domain), or FAE1, an endoplasmic reticulum membrane anchoring domain, results in moderate increases in enzyme activity. Fusing a hemagglutinin epitope tag upstream of an endogenous C-terminal KEK motif results in a significant loss of activity compared to the un-tagged construct, indicating that the endogenous KEK C-terminal di-lysine motif is capable of directing in yeast the ER-retention of this normally plastidial-located protein
additional information
generation of knockout mutants of gene OsFAD8, fatty acids contents (mol%) in leaves from wild-type rice and osfad8 mutant lines at 4°C and 28°C, overview
additional information
the predicted N-terminal plastidial signal peptide of fad7 gene is replaced by an endoplasmic reticulum signal peptide and an endoplasmic reticulum retention signal is placed at the C-terminal, enhancement of alpha-linolenic acid content in transgenic tobacco seeds by targeting the plastidial omega-3 fatty acid desaturase (fad7) gene from Sesamum indicum to the endoplasmic reticulum
additional information
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the predicted N-terminal plastidial signal peptide of fad7 gene is replaced by an endoplasmic reticulum signal peptide and an endoplasmic reticulum retention signal is placed at the C-terminal, enhancement of alpha-linolenic acid content in transgenic tobacco seeds by targeting the plastidial omega-3 fatty acid desaturase (fad7) gene from Sesamum indicum to the endoplasmic reticulum
additional information
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the predicted N-terminal plastidial signal peptide of fad7 gene is replaced by an endoplasmic reticulum signal peptide and an endoplasmic reticulum retention signal is placed at the C-terminal, enhancement of alpha-linolenic acid content in transgenic tobacco seeds by targeting the plastidial omega-3 fatty acid desaturase (fad7) gene from Sesamum indicum to the endoplasmic reticulum
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gene fad7, construction of cDNA and genomic DNA libraries, and screening using Arabidopsis thaliana gene fad7 as template, the genomic clone has 8 exons, DNA and amino acid sequence determination and analysis, genomic organization, phylogenetic analysis
gene fad7, DNA and amino acid sequence determination and analysis
gene fad7, DNA and amino acid sequence determination and analysis using gene fad3 as template. The fad7 and fad8 gene products are functionally equivalent, although the two genes share only about 75% nucleotide identity
gene FAD7, DNA and amino acid sequence determination and analysis, genotyping of wild-type and mutants
gene FAD7, DNA and amino acid sequence determination and analysis, genotyping, expression of T286 enzyme mutants
gene fad7, DNA and amino acid sequence determination and analysis, sequence comparisons,quantitative real-time PCR enzyme expression analysis, phylogenetic analysis
gene fad7, enzyme expression analysis, recombinant expression of fad7 in wild-type Rschew ecotype WF11 cell line and enzyme-deficient mutant cell line SH10 derived from JB101/Col-0
gene FAD7, expression of the -825 Arabidopsis FAD7 promoter-P-glucuronidase fusion gene in Nicotiana tabacum cv. W38
gene fad7, expression of wild-type and chimeric mutant enzymes with or without a c-Myc epitope tag in transgenic Arabidopsis thaliana plants
gene fad7, gene expression profiles, overview. The FAD7 gene expression is differentially regulated in tomato varieties Gerry and T47657 under the effect of cold stress in the short and long term
gene fad7, recombinant expression in Nicotiana tabacum cv. SR1 leaves, that contain increased levels of 16:3 and 18:3 fatty acids, and correspondingly decreased levels of their precursors, hexadecadienoic and linoleic acids, via using Agrobacterium tumefaciens C58ClRif (pGV2280) containing the plasmid pTiDES7 or p501-17. The expression of FAD7 leads to reduced suppression of leaf growth at 1°C compared to wild-type plants. The low-temperature-induced chlorosis is also much reduced in the plants transformed with the fad7 gene. Control growth at 25°C
gene fad7, sequence comparison with FAD3, recombinant expression in Saccharomyces cerevisiae strain W303-1A, plastidial omega3-fatty acid desaturase contains the signalling determinants required for targeting to, and retention in, the endoplasmic reticulum membrane in Saccharomyces cerevisiae but requires co-expressed ferredoxin for activity. Heterologous enzyme expression in yeast shows low activity in contrast to similar expression of microsomal FAD3 omega 3-desaturases. Expression of enzyme variants N-terminally tagged with HA, and/or anchor domains ELO or FAE, and containing a KKNL motif at the C-terminus. Deletion of the endogenous KEK C-terminal motif results in dramatically reduced accumulation of FAD7-HA. Coexpression of ferredoxin
gene fad7, sequence comparisons, recombinant functional expression in Nicotiana tabacum cv. Jayanti seeds and leaves targeted to the endoplasmic reticulum, using the Agrobacterium tumefaciens strain EHA105 transfection method and the binary vector pCAMBIA1300 with CaMV35S promoter, quantitative real-time PCR expression analysis
gene fad7, the promoter sequence of gene fad7 contains several short sequence cis-elements and the -825 bp regulatory region, analysis, overview
gene fad7, two splicing variants fad7-1 and fad7-2, DNA and amino acid sequence determination and analysis, single gene, transcriptome analysis, sequence comparisons of fad genes, phylogenetic analysis, quantitative real-time and RT-PCR expression analysis, recombinant expression in Saccharomyces cerevisiae strain INVSc1, where pYES2-PfrFAD7-1 transformants produce 18:3 when supplemented with 18:2
gene fad7, two splicing variants fad7-1 and fad7-2, DNA and amino acid sequence determination and analysis, single gene, transcriptome analysis, sequence comparisons of fad genes, phylogenetic analysis, quantitative real-time and RT-PCR expression analysis, recombinant expression in Saccharomyces cerevisiae strain INVSc1, where pYES2-PfrFAD7-2 transformants produce 18:3 when supplemented with 18:2
gene fad8, construction of cDNA and genomic DNA libraries, and screening using Arabidopsis thaliana gene fad7 as template, the genomic clone has 7 exons, DNA and amino acid sequence determination and analysis, genomic organization, phylogenetic analysis
gene fad8, DNA and amino acid sequence determination and analysis
gene fad8, DNA and amino acid sequence determination and analysis using gene fad3 as template, constitutive expression of the fad8 cDNA in transgenic plants of a fad7 mutant JBl01, via Agrobacterium turnefaciens C58 (pGV3101) containing plasmid pBI/fad8 or pBIl2l, results in genetic complementation of the mutation, indicating that the fad7 and fad8 gene products are functionally equivalent. Expression of the fad8 cDNA in transgenic plants often results in the co-suppression of both the endogenous fad7 and fad8 genes in spite of the fact that these two genes share only about 75% nucleotide identity
gene FAD8, DNA and amino acid sequence determination and analysis, genotyping of wild-type and mutants. Recombinant expression of AtFAD8-YFP fusion protein in stable transgenic Arabidopsis thaliana lines and transiently in Nicotinana benthamiana leaves, overexpression of YFP-tagged fad8 in Arabidosis thaliana results in increased 18:3 trienoic fatty acid levels in phospholipids but not in galactolipids
gene fad8, DNA and amino acid sequence determination and analysis, sequence comparisons,quantitative real-time PCR enzyme expression analysis, phylogenetic analysis
gene fad8, expression of wild-type and chimeric mutant enzymes with or without a c-Myc epitope tag in transgenic Arabidopsis thaliana plants
gene fad8, recombinant expression in Nicotiana tabacum BY-2 cells and in transgenic tobacco plants via Agrobacterium-mediated transformation. Co-expression of Arabidopsis thaliana FAD8 and Brassica napus FAD3, EC 1.14.19.25, under the control of the 35S CaMV promoter leads to increase in 18:3, which is compensated mainly by the decrease in 18:2, but is also accompanied by a decrease in oleic acid (18:1). Additionally, there is a small but significant decrease in stearic acid (18:0) which seems to be compensated by an increase in palmitic acid (16:0). In the BY-2-FAD8 cells, the ratio of 18:3 to 18:2 is about twofold higher than that in the BY-2 cells. Fatty acid composition of leaf polar lipids of wild-type and transgenic plants, overview
gene OsFAD8, located on chromosome 7, DNA and amino acid sequence determination and analysis
heterologous expression in Synechocystis sp. PCC 6803
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activation of the FAD7 promoter by local wounding treatments. Wounding induces the expression of the FAD7 gene in rosette leaves (2fold), stems (29fold), and roots(10fold). Significant induction by wounding is observed in the overall tissues of stems and includes trichomes, the epidermis, cortex, vascular system, and the pith of the parenchyma. Strong promoter activity is found preferentially in the vascular tissues of wounded roots. Wound activation of the FAD7 promoter in roots occurs via the octadecanoid pathway, inhibitors salicylic acid and n-propyl gallate strongly suppress the wound activation of the FAD7 promoter in roots but not in leaves or stems. Light attenuates the wound-inducing activity of the FAD7 promoter in roots, although in unwounded roots, illumination does not affect the expression of the FAD7 gene. In unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
at 4°C, the transcript level of CsFAD7 decreases significantly 1 h after the stress and then recovers. After 6 h, the expression level is of CsFAD7 remains at levels below the control (0 h) until 48 h, at -5°C, CsFAD7 decreases significantly and then remains stable until 48 h
at 4°C, the transcript level of CsFAD8 decreases significantly 1 h after the stress and then recovers. After 6 h, the expression level of FAD8 is higher than the control at 24 h, at -5°C, CsFAD8 expression decreases significantly and then remains stable until 48 h
FAD7 is up-regulated by wounding but not by low temperature. Total fatty acid and linolenic acid content are higher both, in wounded and intact leaves of plants exposed to low temperature
FAD8 is up-regulated by cold stress but not by wounding. Total fatty acid and linolenic acid content are higher both, in wounded and intact leaves of plants exposed to low temperature
gene fad7 is rapidly induced in elicitor-treated cell culture leading to an accumulation of mRNA in leaves and as well in fungal infection sites in leaf buds, pathogen invasion induces the enzyme
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glycine betaine induces the enzyme expression in tomato plants at low temperature
high-salt treatment induces the accumulation of the ZmFAD7 transcript in roots but drought and abscisic acid have no effect on its expression. Cycloheximide induces the accumulation of the ZmFAD7 transcript in roots
high-salt treatment induces the accumulation of the ZmFAD8 transcript in roots but drought and abscisic acid have no effect on its expression
in unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
in wild-type plants cold-acclimated at 4°C, the transcript levels of OsFAD8 increase significantly, and the expression levels increase in comparison to those of wild-type and of genes OsFAD7 and OsFAD3. OsFAD8 is a cold-inducible gene
induced by low temperature
salt stress induces the enzyme FAD7 in roots
salt stress induces the enzyme FAD8 in roots, the enzyme is induced in leaves by low temperature below 20°C
temperature-sensitive FAD8 expression
the enzyme is induced by wounding in leaves, stems and roots, jasmonic acid induces the enzyme in roots
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the enzyme is significantly induced by wounding in tubers
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the steady-state level of fad8 mRNA is strongly increased in plants grown at low temperature
wounding and abscisic acid induce the enzyme
wounding and abscisic acid induce the enzyme rapidly, while the expression drops below control afterwards
wounding induces the enzyme expression in leaves and roots. The enzyme FAD8 is induced by cold temperatures below 20°C
wounding induces the FAD7 enzyme expression in leaves and roots. Light-responsive gene fad7 shows light-induced accumulation in rosette leaves
activation of the FAD7 promoter by local wounding treatments. Wounding induces the expression of the FAD7 gene in rosette leaves (2fold), stems (29fold), and roots(10fold). Significant induction by wounding is observed in the overall tissues of stems and includes trichomes, the epidermis, cortex, vascular system, and the pith of the parenchyma. Strong promoter activity is found preferentially in the vascular tissues of wounded roots. Wound activation of the FAD7 promoter in roots occurs via the octadecanoid pathway, inhibitors salicylic acid and n-propyl gallate strongly suppress the wound activation of the FAD7 promoter in roots but not in leaves or stems. Light attenuates the wound-inducing activity of the FAD7 promoter in roots, although in unwounded roots, illumination does not affect the expression of the FAD7 gene. In unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
activation of the FAD7 promoter by local wounding treatments. Wounding induces the expression of the FAD7 gene in rosette leaves (2fold), stems (29fold), and roots(10fold). Significant induction by wounding is observed in the overall tissues of stems and includes trichomes, the epidermis, cortex, vascular system, and the pith of the parenchyma. Strong promoter activity is found preferentially in the vascular tissues of wounded roots. Wound activation of the FAD7 promoter in roots occurs via the octadecanoid pathway, inhibitors salicylic acid and n-propyl gallate strongly suppress the wound activation of the FAD7 promoter in roots but not in leaves or stems. Light attenuates the wound-inducing activity of the FAD7 promoter in roots, although in unwounded roots, illumination does not affect the expression of the FAD7 gene. In unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
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high-salt treatment induces the accumulation of the ZmFAD7 transcript in roots but drought and abscisic acid have no effect on its expression. Cycloheximide induces the accumulation of the ZmFAD7 transcript in roots
high-salt treatment induces the accumulation of the ZmFAD7 transcript in roots but drought and abscisic acid have no effect on its expression. Cycloheximide induces the accumulation of the ZmFAD7 transcript in roots
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high-salt treatment induces the accumulation of the ZmFAD8 transcript in roots but drought and abscisic acid have no effect on its expression
high-salt treatment induces the accumulation of the ZmFAD8 transcript in roots but drought and abscisic acid have no effect on its expression
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in unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
in unwounded plants, exogenously applied methyl jasmonate activates the FAD7 promoter in roots, whereas it represses FAD7 promoter activity in leaves
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temperature-sensitive FAD8 expression
temperature-sensitive FAD8 expression
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the steady-state level of fad8 mRNA is strongly increased in plants grown at low temperature
the steady-state level of fad8 mRNA is strongly increased in plants grown at low temperature
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Iba, K.; Gibson, S.; Nishiuchi, T.; Fuse, T.; Nishimura, M.; Arondel, V.; Hugly, S.; Somerville, C.
A gene encoding a chloroplast omega-3 fatty acid desaturase complements alterations in fatty acid desaturation and chloroplast copy number of the fad7 mutant of Arabidopsis thaliana
J. Biol. Chem.
268
24099-24105
1993
Arabidopsis thaliana (P46310)
brenda
Venegas-Caleron, M.; Muro-Pastor, A.M.; Garces, R.; Martinez-Force, E.
Functional characterization of a plastidial omega-3 desaturase from sunflower (Helianthus annuus) in cyanobacteria
Plant Physiol. Biochem.
44
517-525
2006
Helianthus annuus (Q56VS4)
brenda
McConn, M.; Hugly, S.; Browse, J.; Somerville, C.
A Mutation at the fad8 locus of Arabidopsis identifies a second chloroplast [omega]-3 desaturase
Plant Physiol.
106
1609-1614
1994
Arabidopsis thaliana (P46310), Arabidopsis thaliana (P48622)
brenda
Lim, J.M.; Vikramathithan, J.; Hwangbo, K.; Ahn, J.W.; Park, Y.I.; Choi, D.W.; Jeong, W.J.
Threonine 286 of fatty acid desaturase 7 is essential for ?-3 fatty acid desaturation in the green microalga Chlamydomonas reinhardtii
Front. Microbiol.
6
66
2015
Chlamydomonas reinhardtii (A8HMC4), Chlamydomonas reinhardtii
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Teixeira, M.; Carvalho, I.; Brodelius, M.
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Matsuda, O.; Sakamoto, H.; Hashimoto, T.; Iba, K.
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Nishiuchi, T.; Iba, K.
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Kusumi, J.; Iba, K.
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Arabidopsis thaliana (P46310), Arabidopsis thaliana Col-0 (P46310)
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Karabudak, T.; Bor, M.; Oezdemir, F.; Tuerkan, I.
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Solanum lycopersicum (Q7X7I9), Solanum lycopersicum
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Roman, A.; Hernandez, M.L.; Soria-Garcia, A.; Lopez-Gomollon, S.; Lagunas, B.; Picorel, R.; Martinez-Rivas, J.M.; Alfonso, M.
Non-redundant contribution of the plastidial FAD8 omega-3 desaturase to glycerolipid unsaturation at different temperatures in Arabidopsis
Mol. Plant
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Arabidopsis thaliana (P46310), Arabidopsis thaliana (P48622), Arabidopsis thaliana Col-0 (P46310), Arabidopsis thaliana Col-0 (P48622)
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Venegas-Caleron, M.; Beaudoin, F.; Garces, R.; Napier, J.A.; Martinez-Force, E.
The sunflower plastidial omega3-fatty acid desaturase (HaFAD7) contains the signalling determinants required for targeting to, and retention in, the endoplasmic reticulum membrane in yeast but requires co-expressed ferredoxin for activity
Phytochemistry
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Helianthus annuus (Q56VS4), Helianthus annuus
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Nishiuchi, T.; Hamada, T.; Kodama, H.; Iba, K.
Wounding changes the spatial expression pattern of the arabidopsis plastid omega-3 fatty acid desaturase gene (FAD7) through different signal transduction pathways
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Arabidopsis thaliana (P46310), Arabidopsis thaliana Col-0 (P46310)
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Zhang, M.; Barg, R.; Yin, M.; Gueta-Dahan, Y.; Leikin-Frenkel, A.; Salts, Y.; Shabtai, S.; Ben-Hayyim, G.
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Arabidopsis thaliana (P48622), Arabidopsis thaliana Col-0 (P48622)
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Chaturvedi, R.; Krothapalli, K.; Makandar, R.; Nandi, A.; Sparks, A.A.; Roth, M.R.; Welti, R.; Shah, J.
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Arabidopsis thaliana (P46310), Arabidopsis thaliana
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Arabidopsis thaliana (P46310), Arabidopsis thaliana Col-0 (P46310)
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Gibson, S.; Arondel, V.; Iba, K.; Somerville, C.
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Arabidopsis thaliana (P46310), Arabidopsis thaliana (P48622), Arabidopsis thaliana Col-0 (P46310), Arabidopsis thaliana Col-0 (P48622)
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In situ molecular identification of the plastid omega3 fatty acid desaturase FAD7 from soybean: evidence of thylakoid membrane localization
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Glycine max (C4MH52), Glycine max
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Horiguchi, G.; Kodama, H.; Nishimura, M.; Iba, K.
Role of omega-3 fatty acid desaturases in the regulation of the level of trienoic fatty acids during leaf cell maturation
Planta
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Arabidopsis thaliana (P46310), Arabidopsis thaliana Col-0 (P46310)
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Ma, Q.; You, E.; Wang, J.; Wang, Y.; Ding, Z.
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Camellia sinensis (L0GGK2), Camellia sinensis (S5GIT3)
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Roman, A.; Hernandez, M.L.; Soria-Garcia, A.; Lopez-Gomollon, S.; Lagunas, B.; Picorel, R.; Martinez-Rivas, J.M.; Alfonso, M.
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Mol. Plant
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2015
Arabidopsis thaliana (P46310), Arabidopsis thaliana Col-0 (P46310)
brenda
Bhunia, R.K.; Chakraborty, A.; Kaur, R.; Maiti, M.K.; Sen, S.K.
Enhancement of alpha-linolenic acid content in transgenic tobacco seeds by targeting a plastidial omega-3 fatty acid desaturase (fad7) gene of Sesamum indicum to ER
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Sesamum indicum (P48620), Sesamum indicum, Sesamum indicum Var-9 (P48620)
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Lee, K.R.; Lee, Y.; Kim, E.H.; Lee, S.B.; Roh, K.H.; Kim, J.B.; Kang, H.C.; Kim, H.U.
Functional identification of oleate 12-desaturase and omega-3 fatty acid desaturase genes from Perilla frutescens var. frutescens
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Perilla frutescens var. frutescens, Perilla frutescens var. frutescens (A0A190ZLB9)
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Tovuu, A.; Zulfugarov, I.S.; Wu, G.; Kang, I.S.; Kim, C.; Moon, B.Y.; An, G.; Lee, C.H.
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Oryza sativa Japonica Group (Q84NP3)
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