Acyl-CoA:Lysophosphatidylethanolamine Acyltransferase Activity Regulates Growth of Arabidopsis1
The activity of LPEAT affects the growth of Arabidopsis and is essential for maintaining an adequate level of PE, LPE, and LPC in the cells. Arabidopsis ( Arabidopsis thaliana ) contains two enzymes (encoded by the At1g80950 and At2g45670 genes) preferentially acylating lysophosphatidylethanolamine...
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Published in | Plant physiology (Bethesda) Vol. 174; no. 2; pp. 986 - 998 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
American Society of Plant Biologists
13.04.2017
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Online Access | Get full text |
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Abstract | The activity of LPEAT affects the growth of Arabidopsis and is essential for maintaining an adequate level of PE, LPE, and LPC in the cells.
Arabidopsis (
Arabidopsis thaliana
) contains two enzymes (encoded by the
At1g80950
and
At2g45670
genes) preferentially acylating lysophosphatidylethanolamine (
LPE
) with acyl-coenzyme A (CoA), designated LYSOPHOSPHATIDYLETHANOLAMINE ACYLTRANSFERASE1 (LPEAT1) and LPEAT2. The transfer DNA insertion mutant lpeat2 and the double mutant lpeat1 lpeat2 showed impaired growth, smaller leaves, shorter roots, less seed setting, and reduced lipid content per fresh weight in roots and seeds and large increases in
LPE
and lysophosphatidylcholine (
LPC
) contents in leaves. Microsomal preparations from leaves of these mutants showed around 70% decrease in acylation activity of
LPE
with 16:0-CoA compared with wild-type membranes, whereas the acylation with 18:1-CoA was much less affected, demonstrating that other lysophospholipid acyltransferases than the two LPEATs could acylate
LPE
. The above-mentioned effects were less pronounced in the single lpeat1 mutant. Overexpression of either LPEAT1 or LPEAT2 under the control of the 35S promotor led to morphological changes opposite to what was seen in the transfer DNA mutants. Acyl specificity studies showed that LPEAT1 utilized 16:0-CoA at the highest rate of 11 tested acyl-CoAs, whereas LPEAT2 utilized 20:0-CoA as the best acyl donor. Both LPEATs could acylate either
sn
position of ether analogs of
LPC
. The data show that the activities of LPEAT1 and LPEAT2 are, in a complementary way, involved in growth regulation in Arabidopsis. It is shown that LPEAT activity (especially LPEAT2) is essential for maintaining adequate levels of phosphatidylethanolamine,
LPE
, and
LPC
in the cells. |
---|---|
AbstractList | The activity of LPEAT affects the growth of Arabidopsis and is essential for maintaining an adequate level of PE, LPE, and LPC in the cells.
Arabidopsis (
Arabidopsis thaliana
) contains two enzymes (encoded by the
At1g80950
and
At2g45670
genes) preferentially acylating lysophosphatidylethanolamine (
LPE
) with acyl-coenzyme A (CoA), designated LYSOPHOSPHATIDYLETHANOLAMINE ACYLTRANSFERASE1 (LPEAT1) and LPEAT2. The transfer DNA insertion mutant lpeat2 and the double mutant lpeat1 lpeat2 showed impaired growth, smaller leaves, shorter roots, less seed setting, and reduced lipid content per fresh weight in roots and seeds and large increases in
LPE
and lysophosphatidylcholine (
LPC
) contents in leaves. Microsomal preparations from leaves of these mutants showed around 70% decrease in acylation activity of
LPE
with 16:0-CoA compared with wild-type membranes, whereas the acylation with 18:1-CoA was much less affected, demonstrating that other lysophospholipid acyltransferases than the two LPEATs could acylate
LPE
. The above-mentioned effects were less pronounced in the single lpeat1 mutant. Overexpression of either LPEAT1 or LPEAT2 under the control of the 35S promotor led to morphological changes opposite to what was seen in the transfer DNA mutants. Acyl specificity studies showed that LPEAT1 utilized 16:0-CoA at the highest rate of 11 tested acyl-CoAs, whereas LPEAT2 utilized 20:0-CoA as the best acyl donor. Both LPEATs could acylate either
sn
position of ether analogs of
LPC
. The data show that the activities of LPEAT1 and LPEAT2 are, in a complementary way, involved in growth regulation in Arabidopsis. It is shown that LPEAT activity (especially LPEAT2) is essential for maintaining adequate levels of phosphatidylethanolamine,
LPE
, and
LPC
in the cells. |
Author | Stymne, Sten Carlsson, Anders S. Jasieniecka-Gazarkiewicz, Katarzyna Gutbrod, Katharina Peisker, Helga Dörmann, Peter Lager, Ida Banaś, Antoni |
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Copyright | 2017 American Society of Plant Biologists. All Rights Reserved. 2017 |
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Notes | www.plantphysiol.org/cgi/doi/10.1104/pp.17.00391 The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Antoni Banaś (antoni.banas@biotech.ug.edu.pl). |
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Title | Acyl-CoA:Lysophosphatidylethanolamine Acyltransferase Activity Regulates Growth of Arabidopsis1 |
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