Identification of wheat non-specific lipid transfer proteins involved in chilling tolerance

Yu, Guanghui; Hou, Wenqian; Du, Xuye; Wang, Liang; Wu, Hongyan; Zhao, Lanfei; Kong, Lingrang; Wang, Hongwei

doi:10.1007/s00299-014-1655-y

Cited by 24 publications

(19 citation statements)

References 41 publications

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“…A more encyclopedic review on plant LTPs was published rather recently (2). Nevertheless, it is important to also here point out thatLTPs are suggested to be involved in many other processes in plants, such as signalling (34, 35), defence against biotic hazards (36-40) and tolerance to abiotic stresses just to mention a few examples (12,(41)(42)(43)(44)(45)). …”

mentioning

confidence: 99%

Plant lipid transfer proteins: are we finally closing in on the roles of these enigmatic proteins?

Edqvist

Blomqvist

Nieuwland

et al. 2018

Journal of Lipid Research

100

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The nonspecific lipid transfer proteins (LTPs) are small, compact proteins folded around a tunnel-like hydrophobic cavity, making them suitable for lipid binding and transport. LTPs are encoded by large gene families in all land plants, but they have not been identified in algae or any other organisms. Thus, LTPs are considered key proteins for plant survival on and colonization of land. LTPs are abundantly expressed in most plant tissues, both above and below ground. They are usually localized to extracellular spaces outside the plasma membrane. Although the in vivo functions of LTPs remain unclear, accumulating evidence suggests a role for LTPs in the transfer and deposition of monomers required for assembly of the water-proof lipid barriers-such as cutin and cuticular wax, suberin, and sporopolleninformed on many plant surfaces. Some LTPs may be involved in other processes, such as signaling during pathogen attacks. Here, we present the current status of LTP research with a focus on the role of these proteins in lipid barrier deposition and cell expansion. We suggest that LTPs facilitate extracellular transfer of barrier materials and adhesion between barriers and extracellular materials. A growing body of research may uncover the true role of LTPs in plants. Overview of plant non-specific lipid transfer proteinsThe plant non-specific lipid transfer proteins (LTPs) are abundant, secreted, soluble, cysteinerich and small proteins with a molecular size usually below 10 kDa (1, 2). In the LTPs four conserved disulfide bridges, formed by an eight-Cys motif (8CM) with the general form CXn-C-Xn-CC-Xn-CXC-Xn-C-Xn-C, stabilize the folding of four or five α-helices into a very compact 3D-structure (3, 4 and Fig. 1). The folding of the helices results in a central hydrophobic cleft suitable for the binding of hydrophobic ligands, such as fatty acids and other lipids (Fig. 2). The compact structure renders the LTPs very insensitive to heat and denaturing agents (5, 6). LTPs are expressed in all investigated land plants, but have not been detected in any other organisms (7). LTPs are encoded by large gene families in seed plants (2,(8)(9)(10)(11). In bryophytes and ferns the gene families are significantly smaller (7,12). LTPs are classified in five major types (LTP1, LTP2, LTPc, LTPd and LTPg) and four minor types (LTPe, LTPf, LTPh, LTPj and LTPk) (7). The classification is based on the spacing between the Cys residues in the 8CM, the polypeptide sequence identity and the position of evolutionary conserved introns. The classification also reflects post-translational modifications, e.g. LTPs with a GPI-anchor belong to LTPg. LTPd and LTPg are encoded in all land plants which suggests that these were possibly the first LTP types that evolved in land plants. The most well-studied LTP types in flowering plants LTP1 and LTP2 probably evolved later since these are not found in liverworts, mosses or other non-seed plants (7). The LTPs are translated with an N-terminal signal peptide that has a potential to localize th...

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mentioning

confidence: 99%

Plant lipid transfer proteins: are we finally closing in on the roles of these enigmatic proteins?

Edqvist

Blomqvist

Nieuwland

et al. 2018

Journal of Lipid Research

100

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“…When deleted to position −297 bp (−297 TaLTP1::uidA construct), the activity in true leaves disappeared completely, but cotyledon expression was not obviously altered until the promoter region was shortened to position −247 bp ( Figure 1c13-c15,c19-c21). Epidermis-specific expression of nsLTPs has been reported for both dicot and monocot plants [12,18,20,32]. Here, we also transformed promoter deletion constructs −400TaLTP1::uidA, −343TaLTP1::uidA, −297TaLTP1::uidA, −247TaLTP1::uidA into a monocot, B. distachyon ( Figure 1c4-c6,c10-c12,c16-c18,c22-c24).…”

Section: Mapping Of a 5'upstream Region Regulating Epidermis-specificmentioning

confidence: 86%

Molecular Dissection of TaLTP1 Promoter Reveals Functional Cis-Elements Regulating Epidermis-Specific Expression

Wang¹,

Yu²,

Hao

et al. 2020

IJMS

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Plant epidermis serves important functions in shoot growth, plant defense and lipid metabolism, though mechanisms of related transcriptional regulation are largely unknown. Here, we identified cis-elements specific to shoot epidermis expression by dissecting the promoter of Triticum aestivum lipid transfer protein 1 (TaLTP1). A preliminary promoter deletion analysis revealed that a truncated fragment within 400 bp upstream from the translation start site was sufficient to confer conserved epidermis-specific expression in transgenic Brachypodium distachyon and Arabidopsis thaliana. Further, deletion or mutation of a GC(N4)GGCC motif at position −380 bp caused a loss of expression in pavement cells. With an electrophoretic mobility shift assay (EMSA) and transgenic reporter assay, we found that a light-responsive CcATC motif at position −268 bp was also involved in regulating pavement cell-specific expression that is evolutionary conserved. Moreover, expression specific to leaf trichome cells was found to be independently regulated by a CCaacAt motif at position −303 bp.

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“…Significantly increased expression of TaDIR1-2 under low temperature (4°C) treatment suggests the involvement of TaDIR1-2 in enhancing plant acclimation to abiotic stresses. Cold-inducible expression of LTPs in wheat (Yu et al, 2014), rice (Guo C. et al, 2013), maize (Wei and Zhong, 2014), and Arabidopsis (Xu et al, 2011), indicated that LTPs are strongly associated with cold tolerance in higher plants. It is possible that TaDIR1-2 contributes to cold tolerance by interacting with other proteins to modulate defense responses to abiotic stresses in a ROS-dependent manner.…”

Section: Discussionmentioning

confidence: 99%

TaDIR1-2, a Wheat Ortholog of Lipid Transfer Protein AtDIR1 Contributes to Negative Regulation of Wheat Resistance against Puccinia striiformis f. sp. tritici

et al. 2017

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Very few LTPs have been shown to act through plasma membrane receptors or to be involved in the hypersensitive response (HR). DIR1, a new type of plant LTP interacts with lipids in vitro, moves to distant tissues during systemic acquired resistance (SAR) and therefore is thought to be involved in long-distance signaling during SAR. However, the exact functions of DIR1 orthologs in cereal species under biotic and abiotic stresses have not been thoroughly defined. In this study, a novel wheat ortholog of the DIR1 gene, TaDIR1-2, was isolated from Suwon11, a Chinese cultivar of wheat and functionally characterized. Phylogenetic analysis indicated that TaDIR1-2 is clustered within the nsLTP-Type II group and shows a closer relationship with DIR1 orthologs from monocots than from eudicots. TaDIR1-2 was localized in the cytoplasm and the cell membrane of wheat mesophyll protoplast. Transcription of TaDIR1-2 was detected in wheat roots, stems and leaves. TaDIR1-2 transcript was significantly induced during the compatible interaction of wheat with the stripe rust pathogen, Puccinia striiformis f. sp. tritici (Pst). Treatments with salicylic acid (SA) and low temperature significantly up-regulated the expression of TaDIR1-2. Transient overexpression of TaDIR1-2 did not induce cell death or suppress Bax-induced cell death in tobacco leaves. Knocking down the expression of TaDIR1-2 through virus-induced gene silencing increased wheat resistance to Pst accompanied by HR, increased accumulation of H2O2 and SA, increased expression of TaPR1, TaPR2, TaPAL, and TaNOX, and decreased expression of two reactive oxygen species (ROS) scavenging genes TaCAT and TaSOD. Our results suggest that TaDIR1-2 acts as a negative regulator in wheat resistance to Pst by modulating ROS and/or SA-induced signaling.

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Identification of wheat non-specific lipid transfer proteins involved in chilling tolerance

Cited by 24 publications

References 41 publications

Plant lipid transfer proteins: are we finally closing in on the roles of these enigmatic proteins?

Plant lipid transfer proteins: are we finally closing in on the roles of these enigmatic proteins?

Molecular Dissection of TaLTP1 Promoter Reveals Functional Cis-Elements Regulating Epidermis-Specific Expression

TaDIR1-2, a Wheat Ortholog of Lipid Transfer Protein AtDIR1 Contributes to Negative Regulation of Wheat Resistance against Puccinia striiformis f. sp. tritici

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