Abstract

Diacylglycerolpyrophosphate (DGPP) is phosphorylated phosphatidic acid (PA). In plants under stress-free conditions it is present in untraceable amounts. Whereas under stress, induced by either biotic or abiotic factors, plants respond via several signaling cascades ultimately leading to the development of alternative survival strategies. Invariably these signaling cascades involve regulating lipid metabolism. DGPP is one such lipid that is rapidly and transiently elevated under stress conditions, following a stress-induced rise in PA levels. We can speculate that the role of DGPP may be to attenuate PA levels, but this is largely untested. We have previously investigated the physical chemistry of DGPP and showed that the charge of the phosphomonoester is higher than PA. In addition, the spontaneous curvature is zero whereas PA has a negative curvature. Here we examined the lipid-protein interactions between DGPP and proteins that bind to PA to answer the question: is there a co-relation between PA and DGPP based on the proteins that these two lipids bind? The new information on the preference of PA-binding proteins to bind DGPP may begin to answer the question of why PA levels are attenuated with a simultaneous transient increase in DGPP levels. For this study, proteins were chosen from the literature based on stress-stimulated proteins known to bind PA. Liposome binding assays were used to study the affinity of protein binding to PA and DGPP in complex lipid membranes.

Modified Abstract

Diacylglycerolpyrophosphate (DGPP) is phosphorylated phosphatidic acid (PA). Under stress conditions, plants respond via signaling cascades, some involving regulating lipid metabolism. DGPP is a lipid that is elevated under stress, following a stress-induced rise in PA levels. We examined the lipid-protein interactions between DGPP and proteins that bind to PA to analyze a possible co-relation between these two lipids based on the proteins that they bind. The preference of PA-binding proteins to bind DGPP may elucidate why PA levels are attenuated with an increase in DGPP levels. For this study, proteins were chosen from the literature based on stress-stimulated proteins known to bind PA. Liposome binding assays were used to study the affinity of protein binding to PA and DGPP in complex lipid membranes.

Research Category

Biology/Ecology

Primary Author's Major

Biology

Mentor #1 Information

Ms. Priya Putta

Mentor #2 Information

Dr. Edgar E. Kooijman

Presentation Format

Poster

Start Date

21-3-2017 1:00 PM

Research Area

Biology

Included in

Biology Commons

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Mar 21st, 1:00 PM

The effect of lipids on the binding of proteins expressed under stress in plants

Diacylglycerolpyrophosphate (DGPP) is phosphorylated phosphatidic acid (PA). In plants under stress-free conditions it is present in untraceable amounts. Whereas under stress, induced by either biotic or abiotic factors, plants respond via several signaling cascades ultimately leading to the development of alternative survival strategies. Invariably these signaling cascades involve regulating lipid metabolism. DGPP is one such lipid that is rapidly and transiently elevated under stress conditions, following a stress-induced rise in PA levels. We can speculate that the role of DGPP may be to attenuate PA levels, but this is largely untested. We have previously investigated the physical chemistry of DGPP and showed that the charge of the phosphomonoester is higher than PA. In addition, the spontaneous curvature is zero whereas PA has a negative curvature. Here we examined the lipid-protein interactions between DGPP and proteins that bind to PA to answer the question: is there a co-relation between PA and DGPP based on the proteins that these two lipids bind? The new information on the preference of PA-binding proteins to bind DGPP may begin to answer the question of why PA levels are attenuated with a simultaneous transient increase in DGPP levels. For this study, proteins were chosen from the literature based on stress-stimulated proteins known to bind PA. Liposome binding assays were used to study the affinity of protein binding to PA and DGPP in complex lipid membranes.