A sucrose binding protein homologue from soybean affects sucrose uptake in suspension-cultured transgenic tobacco cells

Delú-Filho, Nelson; Pirovani, Carlos Priminho; Pedra, Joao H. F.; Matrangolo, Fabiana S.V.; Macêdo, Joci Neuby Alves; Otoni, Wagner Campos; Fontes, Elizabeth P. B.

doi:10.1016/s0981-9428(00)00752-x

Cited by 21 publications

(24 citation statements)

References 36 publications

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“…RT–PCR assays were performed using gene-specific primers, as previously described 18 . For gene expression analysis by qRT–PCR, gene-specific primers were designed using Primer Express 3.0 (Life Technologies).…”

Section: Methodsmentioning

confidence: 99%

NIK1-mediated translation suppression functions as a plant antiviral immunity mechanism

Zorzatto

Machado

Lopes

et al. 2015

Nature

193

183

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Plants and plant pathogens are subject to continuous co-evolutionary pressure for dominance, and the outcomes of these interactions can substantially impact agriculture and food security1–3. In virus– plant interactions, one of the major mechanisms for plant antiviral immunity relies on RNA silencing, which is often suppressed by co-evolving virus suppressors, thus enhancing viral pathogenicity in susceptible hosts1. In addition, plants use the nucleotide-binding and leucine-rich repeat (NB-LRR) domain-containing resistance proteins, which recognize viral effectors to activate effector-triggered immunity in a defence mechanism similar to that employed in non-viral infections2,3. Unlike most eukaryotic organisms, plants are not known to activate mechanisms of host global translation suppression to fight viruses1,2. Here we demonstrate in Arabidopsis that the constitutive activation of NIK1, a leucine-rich repeat receptor-like kinase (LRR-RLK) identified as a virulence target of the begomovirus nuclear shuttle protein (NSP)4–6, leads to global translation suppression and translocation of the downstream component RPL10 to the nucleus, where it interacts with a newly identified MYB-like protein, L10-INTERACTING MYB DOMAIN-CONTAINING PROTEIN (LIMYB), to downregulate translational machinery genes fully. LIMYB overexpression represses ribosomal protein genes at the transcriptional level, resulting in protein synthesis inhibition, decreased viral messenger RNA association with polysome fractions and enhanced tolerance to begomovirus. By contrast, the loss of LIMYB function releases the repression of translation-related genes and increases susceptibility to virus infection. Therefore, LIMYB links immune receptor LRR-RLK activation to global translation suppression as an antiviral immunity strategy in plants.

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Section: Methodsmentioning

confidence: 99%

NIK1-mediated translation suppression functions as a plant antiviral immunity mechanism

Zorzatto

Machado

Lopes

et al. 2015

Nature

193

183

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“…SuperScript II Kit (Invitrogen) according to the manufacturer's instructions. RT-PCR was performed as described previously (Delú-Filho et al, 2000) with GmNAC-specific primers (Table S2). The presence of contaminating DNA was assessed in control reactions by replacing cDNAs with total RNA preparations.…”

Section: Reverse Transcription-pcr (Rt-pcr)mentioning

confidence: 99%

Complete inventory of soybean NAC transcription factors: Sequence conservation and expression analysis uncover their distinct roles in stress response

Pinheiro

Marques

Costa

et al. 2009

Gene

Self Cite

161

133

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We performed an inventory of soybean NAC transcription factors, in which 101 NAC domain-containing proteins were annotated into 15 different subgroups, showing a clear relationship between structure and function. The six previously described GmNAC proteins (GmNAC1 to GmNAC6) were located in the nucleus and a transactivation assay in yeast confirmed that GmNAC2, GmNAC3, GmNAC4 and GmNAC5 function as transactivators. We also analyzed the expression of the six NAC genes in response to a variety of stress conditions. GmNAC2, GmNAC3 and GmNAC4 were strongly induced by osmotic stress. GmNAC3 and GmNAC4 were also induced by ABA, JA and salinity but differed in their response to cold. Consistent with an involvement in cell death programs, the transient expression of GmNAC1, GmNAC5 and GmNAC6 in tobacco leaves resulted in cell death and enhanced expression of senescence markers. Our results indicate that the described soybean NACs are functionally non-redundant transcription factors involved in response to abiotic stresses and in cell death events in soybean.

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“…In this context, a 62-kD soybean sucrose binding protein (SBP), first isolated by photoaffinity labelling (Ripp et al 1988) and localised to tissues actively engaged in sucrose transport (Grimes et al 1992), was shown to mediate a non-saturable component of sucrose uptake (Overvoorde et al 1996;Delú-Filho et al 2000). However, the latter findings could not be repeated with a faba bean SBP that was shown to be a storage protein .…”

Section: Sugarsmentioning

confidence: 99%

Review: Nutrient loading of developing seeds

Zhang

Zhou

Dibley

et al. 2007

Functional Plant Biol.

177

183

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Abstract. Interest in nutrient loading of seeds is fuelled by its central importance to plant reproductive success and human nutrition. Rates of nutrient loading, imported through the phloem, are regulated by transport and transfer processes located in sources (leaves, stems, reproductive structures), phloem pathway and seed sinks. During the early phases of seed development, most control is likely to be imposed by a low conductive pathway of differentiating phloem cells serving developing seeds. Following the onset of storage product accumulation by seeds, and, depending on nutrient species, dominance of path control gives way to regulation by processes located in sources (nitrogen, sulfur, minor minerals), phloem path (transition elements) or seed sinks (sugars and major mineral elements, such as potassium). Nutrients and accompanying water are imported into maternal seed tissues and unloaded from the conducting sieve elements into an extensive post-phloem symplasmic domain. Nutrients are released from this symplasmic domain into the seed apoplasm by poorly understood membrane transport mechanisms. As seed development progresses, increasing volumes of imported phloem water are recycled back to the parent plant by process(es) yet to be discovered. However, aquaporins concentrated in vascular and surrounding parenchyma cells of legume seed coats could provide a gated pathway of water movement in these tissues. Filial cells, abutting the maternal tissues, take up nutrients from the seed apoplasm by membrane proteins that include sucrose and amino acid/H + symporters functioning in parallel with non-selective cation channels. Filial demand for nutrients, that comprise the major osmotic species, is integrated with their release and phloem import by a turgorhomeostat mechanism located in maternal seed tissues. It is speculated that turgors of maternal unloading cells are sensed by the cytoskeleton and transduced by calcium signalling cascades.

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A sucrose binding protein homologue from soybean affects sucrose uptake in suspension-cultured transgenic tobacco cells

Cited by 21 publications

References 36 publications

NIK1-mediated translation suppression functions as a plant antiviral immunity mechanism

NIK1-mediated translation suppression functions as a plant antiviral immunity mechanism

Complete inventory of soybean NAC transcription factors: Sequence conservation and expression analysis uncover their distinct roles in stress response

Review: Nutrient loading of developing seeds

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