Functional Characterization of the N-Terminal C2 Domain fromArabidopsis thalianaPhospholipase Dαand Dβ

Rahier, Renaud; Noiriel, Alexandre; Abousalham, Abdelkarim

doi:10.1155/2016/2721719

Cited by 11 publications

(7 citation statements)

References 68 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results indicate that also the (His) 6 tag has a great influence on the interfacial binding preference of VpPLD to different phospholipid monolayers. The effect of the (His) 6 tag on the binding and hydrolytic activity of PLD was demonstrated in other studies [24,25,26]. The previous studies and the present results strongly indicate that the effect of the His tag should be taken into consideration when comparing the binding properties or the activities of proteins.…”

Section: Resultssupporting

confidence: 81%

Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus

Wang

Wei

Abousalham

et al. 2018

IJMS

Self Cite

View full text Add to dashboard Cite

The effects of N-terminal (1–34 amino acids) and C-terminal (434–487 amino acids) amino acid sequences on the interfacial binding properties of Phospholipase D from Vibrio parahaemolyticus (VpPLD) were characterized by using monomolecular film technology. Online tools allowed the prediction of the secondary structure of the target N- and C-terminal VpPLD sequences. Various truncated forms of VpPLD with different N- or C-terminal deletions were designed, based on their secondary structure, and their membrane binding properties were examined. The analysis of the maximum insertion pressure (MIP) and synergy factor “a” indicated that the loop structure (1–25 amino acids) in the N-terminal segment of VpPLD had a positive effect on the binding of VpPLD to phospholipid monolayers, especially to 1,2-dimyristoyl-sn-glycero-3-phosphoserine and 1,2-dimyristoyl-sn-glycero-3-phosphocholine. The deletion affecting the N-terminus loop structure caused a significant decrease of the MIP and synergy factor a of the protein for these phospholipid monolayers. Conversely, the deletion of the helix structure (26–34 amino acids) basically had no influence on the binding of VpPLD to phospholipid monolayers. The deletion of the C-terminal amino acids 434–487 did not significantly change the binding selectivity of VpPLD for the various phospholipid monolayer tested here. However, a significant increase of the MIP value for all the phospholipid monolayers strongly indicated that the three-strand segment (434–469 amino acids) had a great negative effect on the interfacial binding to these phospholipid monolayers. The deletion of this peptide caused a significantly greater insertion of the protein into the phospholipid monolayers examined. The present study provides detailed information on the effect of the N- and C-terminal segments of VpPLD on the interfacial binding properties of the enzyme and improves our understanding of the interactions between this enzyme and cell membranes.

show abstract

Section: Resultssupporting

confidence: 81%

Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus

Wang

Wei

Abousalham

et al. 2018

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…One predicted PLD in Chloroidium sp. UTEX 3007 contains several C2 calcium-binding domains, indicating that it acts on membrane phospholipids to produce membrane-bound phosphatidic acid (PA) and cytosolic choline ( Rahier et al, 2016 ). PA has noted roles in environmental stress response ( Peppino Margutti et al, 2017 ), and its liberation has been shown to create ‘supersized’ lipid droplets ( Fei et al, 2011 ).…”

Section: Resultsmentioning

confidence: 99%

The genome and phenome of the green alga Chloroidium sp. UTEX 3007 reveal adaptive traits for desert acclimatization

Nelson

Khraiwesh

et al. 2017

eLife

View full text Add to dashboard Cite

To investigate the phenomic and genomic traits that allow green algae to survive in deserts, we characterized a ubiquitous species, Chloroidium sp. UTEX 3007, which we isolated from multiple locations in the United Arab Emirates (UAE). Metabolomic analyses of Chloroidium sp. UTEX 3007 indicated that the alga accumulates a broad range of carbon sources, including several desiccation tolerance-promoting sugars and unusually large stores of palmitate. Growth assays revealed capacities to grow in salinities from zero to 60 g/L and to grow heterotrophically on >40 distinct carbon sources. Assembly and annotation of genomic reads yielded a 52.5 Mbp genome with 8153 functionally annotated genes. Comparison with other sequenced green algae revealed unique protein families involved in osmotic stress tolerance and saccharide metabolism that support phenomic studies. Our results reveal the robust and flexible biology utilized by a green alga to successfully inhabit a desert coastline.DOI: http://dx.doi.org/10.7554/eLife.25783.001

show abstract

“…For example, Qu et al (2014) discovered that the up-regulated expression of the PLD gene in Vicia faba root tips and Arabidopsis thaliana could induce stomatal closure and H 2 O 2 production (Qu et al 2014). More importantly, Phospholipase D (PLD, EC 3.1.4.4) is a type of lipolytic enzyme that hydrolyzes lecithin, phosphatidylethanolamine, and phosphatidylglycerol under the induction of Ca 2+ , and αPLD also hydrolyzed phosphatidylinositol diphosphate under acidic or Ca 2+ stimulation (Rahier et al 2016). Previous studies have found that calcium signaling deeply involved in the formation of R. glutinosa replanting disease (Yang et al 2015).…”

Section: Discussionmentioning

confidence: 99%

The Role of Root Tissue Membrane Proteins in Replanting Stress in Rehmannia glutinosa

Feng¹

2021

IJAB

View full text Add to dashboard Cite

The perennial herbaceous plant, Rehmannia glutinosa Libosch, is one of traditional Chinese medicines with a long history of cultivation and medicinal use. However, in production of R. glutinosa, replanting disease severely affected its yield and medicinal quality. Replanting disease is the special stress including biotic and abiotic factors. The membrane proteins system plays the important role in process of plants responding to stress factors. In this study, the differentially expressed root tissue membrane proteins between first planted and replanted R. glutinosa were identified through the isobaric tag for relative and absolute quantitation (iTRAQ). As a result, the membrane protein extraction kit could highly effectively extract the membrane proteins from R. glutinosa root tissue. A total of 698 differential membrane proteins between first planted and replanted R. glutinosa were obtained. Functional analysis revealed that the differential membrane proteins were involved in various metabolic pathways, including transport and breakdown, signal transduction, membrane trafficking and environmental response. Two important molecular events that occurred in cellular membrane of replanted R. glutinosa including the imbalance of ROS (Reactive Oxygen Species) metabolism and immune response were identified in this study. When replanted R. glutinosa plants faced the complex environment factors in rhizosphere, the proteins located in cellular membrane were often first activated to response to stress stimulus, resulted in the upregulated expression of a large number of LRR-RLKs (Leucine-rich repeat receptor-like kinases) receptor proteins. Meanwhile, the Ca2+ signal proteins and related receptor proteins transmitted and responded to the replanting stress, which induced severe oxidative stress response in the cell membrane of R. glutinosa, membrane peroxidation, intracellular signal disorder, and eventually produce replanting disease. Our findings provided the theoretical and data foundation for elucidating the key mechanisms associated with replanting stress. © 2021 Friends Science Publishers

show abstract

Functional Characterization of the N-Terminal C2 Domain fromArabidopsis thalianaPhospholipase Dαand Dβ

Cited by 11 publications

References 68 publications

Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus

Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus

The genome and phenome of the green alga Chloroidium sp. UTEX 3007 reveal adaptive traits for desert acclimatization

The Role of Root Tissue Membrane Proteins in Replanting Stress in Rehmannia glutinosa

Contact Info

Product

Resources

About