scholarly journals Redox proteomics of stomatal immunity reveals role of a lipid transfer protein in plant defense

2020 ◽  
Author(s):  
Kelly M Balmant ◽  
Sheldon R Lawrence ◽  
Benjamin V Duong ◽  
Fanzhao Zhu ◽  
Ning Zhu ◽  
...  
Keyword(s):  
Plant Defense ◽  
Lipid Transfer Protein ◽  
Guard Cells ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Redox Proteomics ◽  
Transfer Protein ◽  
Redox Responsive ◽  
Redox Sensors ◽  
Thiol Redox

ABSTRACTRedox-based post-translational modifications (PTMs) involving protein cysteine residues as redox sensors are important to various physiological processes. However, little is known about redox-sensitive proteins in guard cells and their functions in stomatal immunity. In this study, we applied an integrative protein labeling method cysTMTRAQ and identified guard cell proteins that were altered by thiol redox PTMs in response to a bacterial flagellin peptide flg22. In total, eight, seven and 20 potential redox-responsive proteins were identified in guard cells treated with flg22 for 15, 30 and 60 min, respectively. The proteins fall into several functional groups including photosynthesis, lipid binding, oxidation-reduction, and defense. Among the proteins, a lipid transfer protein (LTP)-II was confirmed to be redox-responsive and involved in plant resistance to Pseudomonas syringe pv. tomato DC3000. This study not only creates an inventory of potential redox-sensitive proteins in flg22 signal transduction in guard cells, but also highlights the relevance of the lipid transfer protein in plant defense against the bacterial pathogens.Sentence summaryThiol-redox proteomics identified potential redox sensors important in stomatal immunity, and a lipid transfer protein was characterized to function as a redox sensor in plant immune response.

Guard cell redox proteomics reveals a role of lipid transfer protein in plant defense

2021 ◽  
pp. 104247
Author(s):  
Kelly M. Balmant ◽  
Sheldon R. Lawrence ◽  
Benjamin V. Duong ◽  
Fanzhao Zhu ◽  
Ning Zhu ◽  
...  
Keyword(s):  
Plant Defense ◽  
Guard Cell ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Redox Proteomics ◽  
Transfer Protein

scholarly journals Lipid binding in rice nonspecific lipid transfer protein-1 complexes fromOryza sativa

2004 ◽  
Vol 13 (9) ◽  
pp. 2304-2315 ◽  
Author(s):  
Hui-Chun Cheng ◽  
Pei-Tsung Cheng ◽  
Peiyu Peng ◽  
Ping-Chiang Lyu ◽  
Yuh-Ju Sun
Keyword(s):  
Lipid Transfer Protein ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Nonspecific Lipid Transfer Protein

scholarly journals Phospholipid transfer proteins revisited

1997 ◽  
Vol 324 (2) ◽  
pp. 353-360 ◽  
Author(s):  
Karel. W. A WIRTZ
Keyword(s):  
Mammalian Cells ◽  
Lipid Transfer Protein ◽  
Fusion Reaction ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Cell Functions ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Phosphatidylinositol Transfer

Phosphatidylinositol transfer protein (PI-TP) and the non-specific lipid transfer protein (nsL-TP) (identical with sterol carrier protein 2) belong to the large and diverse family of intracellular lipid-binding proteins. Although these two proteins may express a comparable phospholipid transfer activity in vitro, recent studies in yeast and mammalian cells have indicated that they serve completely different functions. PI-TP (identical with yeast SEC14p) plays an important role in vesicle flow both in the budding reaction from the trans-Golgi network and in the fusion reaction with the plasma membrane. In yeast, vesicle budding is linked to PI-TP regulating Golgi phosphatidylcholine (PC) biosynthesis with the apparent purpose of maintaining an optimal PI/PC ratio of the Golgi complex. In mammalian cells, vesicle flow appears to be dependent on PI-TP stimulating phosphatidylinositol 4,5-bisphosphate (PIP2) synthesis. This latter process may also be linked to the ability of PI-TP to reconstitute the receptor-controlled PIP2-specific phospholipase C activity. The nsL-TP is a peroxisomal protein which, by its ability to bind fatty acyl-CoAs, is most likely involved in the β-oxidation of fatty acids in this organelle. This protein constitutes the N-terminus of the 58 kDa protein which is one of the peroxisomal 3-oxo-acyl-CoA thiolases. Further studies on these and other known phospholipid transfer proteins are bound to reveal new insights in their important role as mediators between lipid metabolism and cell functions.

scholarly journals The Lipid Transfer Protein 1 from Nicotiana benthamiana Assists Bamboo mosaic virus Accumulation

Viruses ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 1361
Author(s):  
Ling-Ying Chiu ◽  
I-Hsuan Chen ◽  
Yau-Heiu Hsu ◽  
Ching-Hsiu Tsai
Keyword(s):  
Virus Infection ◽  
Mosaic Virus ◽  
Nicotiana Benthamiana ◽  
Lipid Transfer Protein ◽  
Lipid Binding ◽  
Host Factors ◽  
Functional Domain ◽  
Lipid Transfer ◽  
Calmodulin Binding ◽  
Transfer Protein

Host factors play a pivotal role in regulating virus infection. Uncovering the mechanism of how host factors are involved in virus infection could pave the way to defeat viral disease. In this study, we characterized a lipid transfer protein, designated NbLTP1 in Nicotiana benthamiana, which was downregulated after Bamboo mosaic virus (BaMV) inoculation. BaMV accumulation significantly decreased in NbLTP1-knockdown leaves and protoplasts compared with the controls. The subcellular localization of the NbLTP1-orange fluorescent protein (OFP) was mainly the extracellular matrix. However, when we removed the signal peptide (NbLTP1/ΔSP-OFP), most of the expressed protein targeted chloroplasts. Both NbLTP1-OFP and NbLTP1/ΔSP-OFP were localized in chloroplasts when we removed the cell wall. These results suggest that NbLTP1 may have a secondary targeting signal. Transient overexpression of NbLTP1 had no effect on BaMV accumulation, but that of NbLTP1/ΔSP significantly increased BaMV expression. NbLTP1 may be a positive regulator of BaMV accumulation especially when its expression is associated with chloroplasts, where BaMV replicates. The mutation was introduced to the predicted phosphorylation site to simulate the phosphorylated status, NbLTP/ΔSP/P(+), which could still assist BaMV accumulation. By contrast, a mutant lacking calmodulin-binding or simulates the phosphorylation-negative status could not support BaMV accumulation. The lipid-binding activity of LTP1 was reported to be associated with calmodulin-binding and phosphorylation, by which the C-terminus functional domain of NbLTP1 may play a critical role in BaMV accumulation.

Lipoprotein assembly and function in an evolutionary perspective

2010 ◽  
Vol 1 (2) ◽  
pp. 165-183 ◽  
Author(s):  
Dick J. Van der Horst ◽  
Kees W. Rodenburg
Keyword(s):  
Lipid Transfer Protein ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Microsomal Triglyceride Transfer Protein ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Density Lipoprotein Receptor ◽  
Exchangeable Basis ◽  
And Function

AbstractCirculatory fat transport in animals relies on members of the large lipid transfer protein (LLTP) superfamily, including mammalian apolipoprotein B (apoB) and insect apolipophorin II/I (apoLp-II/I). ApoB and apoLp-II/I, constituting the structural (non-exchangeable) basis for the assembly of various lipoproteins, acquire lipids through microsomal triglyceride-transfer protein, another LLTP family member, and bind them by means of amphipathic α-helical and β-sheet structural motifs. Comparative research reveals that LLTPs evolved from the earliest animals and highlights the structural adaptations in these lipid-binding proteins. Thus, in contrast to apoB, apoLp-II/I is cleaved post-translationally by a furin, resulting in the appearance of two non-exchangeable apolipoproteins in the single circulatory lipoprotein in insects, high-density lipophorin (HDLp). The remarkable structural similarities between mammalian and insect lipoproteins notwithstanding important functional differences relate to the mechanism of lipid delivery. Whereas in mammals, partial delipidation of apoB-containing lipoproteins eventually results in endocytic uptake of their remnants, mediated by members of the low-density lipoprotein receptor (LDLR) family, and degradation in lysosomes, insect HDLp functions as a reusable lipid shuttle capable of alternate unloading and reloading of lipid. Also, during muscular efforts (flight activity), an HDLp-based lipoprotein shuttle provides for the transport of lipid for energy generation. Although a lipophorin receptor – a homolog of LDLR – was identified that mediates endocytic uptake of HDLp during specific developmental periods, the endocytosed lipoprotein appears to be recycled in a transferrin-like manner. These data highlight that the functional adaptations in the lipoprotein lipid carriers in mammals and insects also emerge with regard to the functioning of their cognate receptors.

scholarly journals High-affinity binding of very-long-chain fatty acyl-CoA esters to the peroxisomal non-specific lipid-transfer protein (sterol carrier protein-2)

1999 ◽  
Vol 339 (1) ◽  
pp. 193-199 ◽  
Author(s):  
Tobias B. DANSEN ◽  
Jan WESTERMAN ◽  
Fred S. WOUTERS ◽  
Ronald J. A. WANDERS ◽  
Arie van HOEK ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Lipid Transfer Protein ◽  
Fatty Acyl ◽  
Lipid Binding ◽  
Tryptophan Residue ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid ◽  
Long Chain ◽  
Lipid Binding Site

Binding of fluorescent fatty acids to bovine liver non-specific lipid-transfer protein (nsL-TP) was assessed by measuring fluorescence resonance energy transfer (FRET) between the single tryptophan residue of nsL-TP and the fluorophore. Upon addition of pyrene dodecanoic acid (Pyr-C12) and cis-parinaric acid to nsL-TP, FRET was observed indicating that these fatty acids were accommodated in the lipid binding site closely positioned to the tryptophan residue. Substantial binding was observed only when these fatty acids were presented in the monomeric form complexed to β-cyclodextrin. As shown by time-resolved fluorescence measurements, translocation of Pyr-C12 from the Pyr-C12–β-cyclodextrin complex to nsL-TP changed dramatically the direct molecular environment of the pyrene moiety: i.e. the fluorescence lifetime of the directly excited pyrene increased at least by 25% and a distinct rotational correlation time of 7 ns was observed. In order to evaluate the affinity of nsL-TP for intermediates of the β-oxidation pathway, a binding assay was developed based on the ability of fatty acyl derivatives to displace Pyr-C12 from the lipid binding site as reflected by the reduction of FRET. Hexadecanoyl-CoA and 2-hexadecenoyl-CoA were found to bind readily to nsL-TP, whereas 3-hydroxyhexadecanoyl-CoA and 3-ketohexadecanoyl-CoA bound poorly. The highest affinities were observed for the very-long-chain fatty acyl-CoA esters (24:0-CoA, 26:0-CoA) and their enoyl derivatives (24:1-CoA, 26:1-CoA). Binding of non-esterified hexadecanoic acid and tetracosanoic acid (24:0) was negligible.

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