AtSUC3, a gene encoding a new Arabidopsis sucrose transporter, is expressed in cells adjacent to the vascular tissue and in a carpel cell layer

Meyer, Stefan; Melzer, Michael; Truernit, Elisabeth; Hümmer, Carola; Besenbeck, Rainer; Stadler, Ruth; Sauer, Norbert

doi:10.1046/j.1365-313x.2000.00934.x

Cited by 109 publications

(39 citation statements)

References 57 publications

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“…However, it cannot be excluded, that the RNA expression pattern as derived from promoter-reporter studies may not entirely reflect the in-vivo protein localization pattern. The expression of SUT2 in companion cells is in disagreement with immunolocalization data in Arabidopsis [24]. …”

Section: Resultsmentioning

confidence: 81%

Interactions between co-expressed Arabidopsis sucrose transporters in the split-ubiquitin system

et al. 2003

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BackgroundThe Arabidopsis genome contains nine sucrose transporter paralogs falling into three clades: SUT1-like, SUT2 and SUT4. The carriers differ in their kinetic properties. Many transport proteins are known to exist as oligomers. The yeast-based split ubiquitin system can be used to analyze the ability of membrane proteins to interact.ResultsPromoter-GUS fusions were used to analyze the cellular expression of the three transporter genes in transgenic Arabidopsis plants. All three fusion genes are co-expressed in companion cells. Protein-protein interactions between Arabidopsis sucrose transporters were tested using the split ubiquitin system. Three paralogous sucrose transporters are capable of interacting as either homo- or heteromers. The interactions are specific, since a potassium channel and a glucose transporter did not show interaction with sucrose transporters. Also the biosynthetic and metabolizing enzymes, sucrose phosphate phosphatase and sucrose synthase, which were found to be at least in part bound to the plasma membrane, did not specifically interact with sucrose transporters.ConclusionsThe split-ubiquitin system provides a powerful tool to detect potential interactions between plant membrane proteins by heterologous expression in yeast, and can be used to screen for interactions with membrane proteins as baits. Like other membrane proteins, the Arabidopsis sucrose transporters are able to form oligomers. The biochemical approaches are required to confirm the in planta interaction.

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Section: Resultsmentioning

confidence: 81%

Interactions between co-expressed Arabidopsis sucrose transporters in the split-ubiquitin system

et al. 2003

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“…Subcellular Localization of CgHXT4 in Baker's Yeast-A CgHXT4-GFP fusion was generated by amplification of the CgHXT4 open reading frame (ORF) with the primers CgHXT4(III)fw and CgHXT4-pEX-GFPr (Table 1) and by insertion of the resulting fragment upstream of the GFP ORF into the pEX-Tag plasmid (19). Subcellular localization of the CgHXT4-GFP fusion in transformed yeast cells (Gietz et al,18) was determined by confocal microscopy (Leica TCS SPII; Leica Microsystems, Bensheim, Germany) as described (6).…”

Section: Methodsmentioning

confidence: 99%

Hexose Transporters of a Hemibiotrophic Plant Pathogen

Lingner

Münch

Deising

et al. 2011

Journal of Biological Chemistry

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Plant pathogenic fungi use a wide range of different strategies to gain access to the carbon sources of their host plants. The hemibiotrophic maize pathogen Colletotrichum graminicola (teleomorph Glomerella graminicola) colonizes its host plants, and, after a short biotrophic phase, switches to destructive, necrotrophic development. Here we present the identification of five hexose transporter genes from C. graminicola, CgHXT1 to CgHXT5, the functional characterization of the encoded proteins, and detailed expression studies for these genes during vegetative and pathogenic development. Whereas CgHXT4 is expressed under all conditions analyzed, transcript abundances of CgHXT1 and CgHXT3 are transiently up-regulated during the biotrophic phase, and CgHXT2 and CgHXT5 are expressed exclusively during necrotrophic development. Analyses of the encoded proteins characterized CgHXT5 as a low-affinity/highcapacity hexose transporter with a narrow substrate specificity for glucose and mannose. In contrast, CgHXT1 to CgHXT3 are high affinity/low capacity transporters that also accept other substrates, including fructose, galactose, or xylose. CgHXT4, the largest of the identified proteins, has only little transport activity and may function as a sugar sensor. Phylogenetic studies revealed hexose transporters closely related to the five CgHXT proteins also in other pathogenic fungi suggesting conserved functions of these proteins during fungal pathogenesis.The ascomycete Colletotrichum graminicola (Cesati) Wilson [teleomorph Glomerella graminicola (Politis)] is the causal agent of the worldwide occurring stem rot and leaf anthracnose of maize (Zea mays). Its hemibiotrophic lifestyle is characterized by an enduring destructive (necrotrophic) development that follows a short non-destructive (biotrophic) period of primary invasion and colonization (1, 2). The primary hyphae formed during this initial biotrophic phase invaginate but do not breach the plasma membrane of the host, as C. graminicola still depends on living host cells for an efficient transfer of nutrients (3). During the necrotrophic phase, however, which is initiated 48 to 72 h postinoculation, fast growing thin secondary hyphae breach the plant plasma membrane, kill the cell, and start to ramify within the host tissue. At the same time, secreted enzymes (4) degrade plant extracellular polysaccharides releasing a variety of mono-, di-, and oligosaccharides that are immediately accessibly for the fungus. Obviously, the fungus will need to respond to the changing carbon environment during these infection stages, to establish different transport systems in its plasma membrane, and to adjust the uptake of organic carbon sources to the changing concentrations and composition of its environment.So far, nothing is known about the carbon sources used by C. graminicola or other hemibiotrophic fungi at these different infection stages or about the transport proteins used for carbon acquisition in infected plant material. However, over the last years plasma membrane-localiz...

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“…Several Type IIB members are plasma membrane-localized, high-affinity transporters (reviewed in Braun and Slewinski, 2009), a striking functional similarity to eudicot-specific Type I SUTs. Like Type IIB, several Type II members are also plasma membrane-localized (Barker et al, 2000; Meyer et al, 2000), but unlike Type IIB, Type II SUTs harbor an extended central cytoplasmic loop with unclear function in both eudicots and monocots (Aoki et al, 2003; Barth et al, 2003; Meyer et al, 2004; Hackel et al, 2006). Type III (Group 4) consists of all known tonoplast SUTs from both monocots and eudicots that are thought to facilitate sucrose release from vacuoles (Eom et al, 2011; Payyavula et al, 2011; Schneider et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Bayesian phylogeny of sucrose transporters: ancient origins, differential expansion and convergent evolution in monocots and dicots

Peng

Xue

et al. 2014

Front. Plant Sci.

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Sucrose transporters (SUTs) are essential for the export and efficient movement of sucrose from source leaves to sink organs in plants. The angiosperm SUT family was previously classified into three or four distinct groups, Types I, II (subgroup IIB), and III, with dicot-specific Type I and monocot-specific Type IIB functioning in phloem loading. To shed light on the underlying drivers of SUT evolution, Bayesian phylogenetic inference was undertaken using 41 sequenced plant genomes, including seven basal lineages at key evolutionary junctures. Our analysis supports four phylogenetically and structurally distinct SUT subfamilies, originating from two ancient groups (AG1 and AG2) that diverged early during terrestrial colonization. In both AG1 and AG2, multiple intron acquisition events in the progenitor vascular plant established the gene structures of modern SUTs. Tonoplastic Type III and plasmalemmal Type II represent evolutionarily conserved descendants of AG1 and AG2, respectively. Type I and Type IIB were previously thought to evolve after the dicot-monocot split. We show, however, that divergence of Type I from Type III SUT predated basal angiosperms, likely associated with evolution of vascular cambium and phloem transport. Type I SUT was subsequently lost in monocots along with vascular cambium, and independent evolution of Type IIB coincided with modified monocot vasculature. Both Type I and Type IIB underwent lineage-specific expansion. In multiple unrelated taxa, the newly-derived SUTs exhibit biased expression in reproductive tissues, suggesting a functional link between phloem loading and reproductive fitness. Convergent evolution of Type I and Type IIB for SUT function in phloem loading and reproductive organs supports the idea that differential vascular development in dicots and monocots is a strong driver for SUT family evolution in angiosperms.

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AtSUC3, a gene encoding a new Arabidopsis sucrose transporter, is expressed in cells adjacent to the vascular tissue and in a carpel cell layer

Cited by 109 publications

References 57 publications

Interactions between co-expressed Arabidopsis sucrose transporters in the split-ubiquitin system

Interactions between co-expressed Arabidopsis sucrose transporters in the split-ubiquitin system

Hexose Transporters of a Hemibiotrophic Plant Pathogen

Bayesian phylogeny of sucrose transporters: ancient origins, differential expansion and convergent evolution in monocots and dicots

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