Proteomics of curcurbit phloem exudate reveals a network of defence proteins

Walz, Christina; Giavalisco, Patrick; Schad, Martina; Juenger, Melanie; Klose, Joachim; Kehr, Julia

doi:10.1016/j.phytochem.2004.04.006

Cited by 207 publications

(196 citation statements)

References 60 publications

Supporting

Mentioning

170

Contrasting

Unclassified

Order By: Relevance

“…From the 27-and 55-kD fractions, we were able to characterize 24 proteins unambiguously (Supplemental Table S3). The relatively high frequency of glutathione S-transferase, dehydroascorbate reductase, catalase, copper ion-binding oxidoreductase, and enolase was consistent with the identification of oxidation-related or redox-related proteins in other reports of phloem sap protein analysis in other species (Walz et al, 2004;Giavalisco et al, 2006;Kehr, 2006). Three of the 24 proteins identified matched with orthologs found in the sap of B. napus: the UDP-Glc pyrophosphorylase UGP2, the glutathione S-transferase GSTF9, and the adenosylhomocysteinase SAHH1/ HOG1 (Giavalisco et al, 2006).…”

Section: Survey Of Phloem Sap Proteinssupporting

confidence: 88%

“…PP2 lectins from cucurbits and the related protein Nictaba have been reported to be dimeric in planta (Read and Northcote, 1983a;Chen et al, 2002;Walz et al, 2004). The existence of a high-affinity site in PP2-A1 dimeric forms is consistent with these observations.…”

Section: Pp2-a1 Is a Glcnac Oligomer-binding Lectin With Two Types Ofsupporting

confidence: 65%

“…We also cannot rule out the possibility that the method used to collect phloem sap, involving the use of EDTA, a chelator of Ca 2+ ions, affects the aggregation and mobility of PP2 proteins. Previous studies identifying PP2 phloem lectins in phloem sap proteomes were based on the collection of sap by phloem bleeding rather than EDTA-facilitated exudation (Walz et al, 2002(Walz et al, , 2004Giavalisco et al, 2006;Lin et al, 2009). Therefore, it remains unclear whether PP2-A1 subunits or small oligomers are mobile in the sieve elements of Arabidopsis or whether they are attached to sieve element membranes or to P-proteins.…”

Section: Survey Of Phloem Sap Proteinsmentioning

confidence: 99%

See 2 more Smart Citations

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

et al. 2010

View full text Add to dashboard Cite

Phloem Protein2 (PP2) is a component of the phloem protein bodies found in sieve elements. We describe here the lectin properties of the Arabidopsis (Arabidopsis thaliana) PP2-A1. Using a recombinant protein produced in Escherichia coli, we demonstrated binding to N-acetylglucosamine oligomers. Glycan array screening showed that PP2-A1 also bound to highmannose N-glycans and 9-acyl-N-acetylneuraminic sialic acid. Fluorescence spectroscopy-based titration experiments revealed that PP2-A1 had two classes of binding site for N,N#,N$-triacetylchitotriose, a low-affinity site and a high-affinity site, promoting the formation of protein dimers. A search for structural similarities revealed that PP2-A1 aligned with the Cbm4 and Cbm22-2 carbohydrate-binding modules, leading to the prediction of a b-strand structure for its conserved domain. We investigated whether PP2-A1 interacted with phloem sap glycoproteins by first characterizing abundant Arabidopsis phloem sap proteins by liquid chromatography-tandem mass spectrometry. Then we demonstrated that PP2-A1 bound to several phloem sap proteins and that this binding was not completely abolished by glycosidase treatment. As many plant lectins have insecticidal activity, we also assessed the effect of PP2-A1 on weight gain and survival in aphids. Unlike other mannosebinding lectins, when added to an artificial diet, recombinant PP2-A1 had no insecticidal properties against Acyrthosiphon pisum and Myzus persicae. However, at mid-range concentrations, the protein affected weight gain in insect nymphs. These results indicate the presence in PP2-A1 of several carbohydrate-binding sites, with potentially different functions in the trafficking of endogenous proteins or in interactions with phloem-feeding insects.

show abstract

Section: Survey Of Phloem Sap Proteinssupporting

confidence: 88%

Section: Pp2-a1 Is a Glcnac Oligomer-binding Lectin With Two Types Ofsupporting

confidence: 65%

Section: Survey Of Phloem Sap Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

et al. 2010

View full text Add to dashboard Cite

show abstract

“…Proteomics analysis of phloem exudates revealed that homologs of ACBP6 exist in cucumber (Cucumis sativus) and pumpkin (Cucurbita maxima; Walz et al, 2004). In rice (Oryza sativa), its homolog is also a major phloem sap protein (Suzui et al, 2006), suggesting that plant 10-kD ACBPs may be associated with longdistance transport (possibly of long-chain acyl-CoA esters) and/or in stress and defense, since phloem proteins primarily belong to these classes (Walz et al, 2004;Suzui et al, 2006).…”

mentioning

confidence: 99%

“…In rice (Oryza sativa), its homolog is also a major phloem sap protein (Suzui et al, 2006), suggesting that plant 10-kD ACBPs may be associated with longdistance transport (possibly of long-chain acyl-CoA esters) and/or in stress and defense, since phloem proteins primarily belong to these classes (Walz et al, 2004;Suzui et al, 2006). Here, we sought to investigate if Arabidopsis ACBP6 expression is responsive to abiotic and biotic stresses.…”

mentioning

confidence: 99%

Overexpression of the Arabidopsis 10-Kilodalton Acyl-Coenzyme A-Binding Protein ACBP6 Enhances Freezing Tolerance

2008

View full text Add to dashboard Cite

Small 10-kD acyl-coenzyme A-binding proteins (ACBPs) are highly conserved proteins that are prevalent in eukaryotes. In Arabidopsis (Arabidopsis thaliana), other than the 10-kD ACBP homolog (designated Arabidopsis ACBP6), there are five larger forms of ACBPs ranging from 37.5 to 73.1 kD. In this study, the cytosolic subcellular localization of Arabidopsis ACBP6 was confirmed by analyses of transgenic Arabidopsis expressing autofluorescence-tagged ACBP6 and western-blot analysis of subcellular fractions using ACBP6-specific antibodies. The expression of Arabidopsis ACBP6 was noticeably induced at 48 h after 4°C treatment by northern-blot analysis and western-blot analysis. Furthermore, an acbp6 T-DNA insertional mutant that lacked ACBP6 mRNA and protein displayed increased sensitivity to freezing temperature (28°C), while ACBP6-overexpressing transgenic Arabidopsis plants were conferred enhanced freezing tolerance. Northern-blot analysis indicated that ACBP6-associated freezing tolerance was not dependent on the induction of cold-regulated COLD-RESPONSIVE gene expression. Instead, ACBP6 overexpressors showed increased expression of mRNA encoding phospholipase Dd. Lipid profiling analyses of rosettes from cold-acclimated, freezingtreated (28°C) transgenic Arabidopsis plants overexpressing ACBP6 showed a decline in phosphatidylcholine (236% and 246%) and an elevation of phosphatidic acid (73% and 67%) in comparison with wild-type plants. From our comparison, the gain in freezing tolerance in ACBP6 overexpressors that was accompanied by decreases in phosphatidylcholine and an accumulation of phosphatidic acid is consistent with previous findings on phospholipase Dd-overexpressing transgenic Arabidopsis. In vitro filterbinding assays indicating that histidine-tagged ACBP6 binds phosphatidylcholine, but not phosphatidic acid or lysophosphatidylcholine, further imply a role for ACBP6 in phospholipid metabolism in Arabidopsis, including the possibility of ACBP6 in the cytosolic trafficking of phosphatidylcholine.

show abstract

Phloem Long‐Distance Trafficking of Proteins and RNAs

Wolf¹

2009

Encyclopedia of Life Sciences

View full text Add to dashboard Cite

Phloem sap contains a wide range of macromolecules, including ribonucleic acids (RNAs) and proteins. Recent advances in genomic and proteomic technologies have enabled the identification of thousands of these macromolecules. However, technical limitations are still the main obstacle to the complete characterization of macromolecule profiles in the sieve tube. Grafting experiments have established that numerous macromolecules are capable of moving long distances between tissues, providing the foundation for the hypothesis of an interorgan information superhighway in higher plants involving the phloem. This chapter presents the current knowledge on proteins and messenger RNA (mRNA) molecules present in the sieve tube. The challenge now is to characterize the biological role of trafficking macromolecules, such as their involvement in the signal‐transduction pathway(s) elicited by environmental cues and in orchestrating developmental processes at the whole‐plant level. Key concepts Phloem sap contains macromolecules such as proteins and RNAs. Protein profiles in the sieve tube are tissue specific. Phloem proteins act as long‐distance signalling molecules. Plant viruses move long distance via the phloem. Endogenous RNA molecules are capable of trafficking long distance via the phloem. mRNA molecules may act as long‐distance signalling molecules.

show abstract

Proteomics of curcurbit phloem exudate reveals a network of defence proteins

Cited by 207 publications

References 60 publications

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

Overexpression of the Arabidopsis 10-Kilodalton Acyl-Coenzyme A-Binding Protein ACBP6 Enhances Freezing Tolerance

Phloem Long‐Distance Trafficking of Proteins and RNAs

Contact Info

Product

Resources

About