Nucleocytoplasmic plant lectins

Lannoo, Nausicaä; Damme, Els J.M. Van

doi:10.1016/j.bbagen.2009.07.021

Cited by 111 publications

(107 citation statements)

References 151 publications

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“…Like the inducible lectins (Lannoo and Van Damme, 2010), AtJAC1 is a nucleocytoplasmic protein (Supplemental Fig. S4A).…”

Section: Jacalin-lectins Interact With Rna-binding Proteins and Regulmentioning

confidence: 99%

“…(Nagano et al, 2008), 31 in rice (Jiang et al, 2010), and 67 in wheat (Song et al, 2013b). Beyond the classic lectins (Lannoo and Van Damme, 2010), as defined by characteristics such as high expression in storage organs, distribution in extracellular compartments, and recognition of exogenous carbohydrate or glycoprotein, increasing numbers of inducible JRLs were reported to be important in the regulation of plant development as well as biotic and abiotic stress responses (for review, see Lannoo and Van Damme, 2010). Our data here revealed that the Jacalin-lectin AtJAC1/JRL35 (Nagano et al, 2008) regulates the transition of flowering in Arabidopsis.…”

Section: Grp7bsmentioning

confidence: 99%

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AtJAC1 Regulates Nuclear Accumulation of GRP7, Influencing RNA Processing of FLC Antisense Transcripts and Flowering Time in Arabidopsis

Xiao

et al. 2015

Plant Physiol.

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Lectins selectively recognize sugars or glycans for defense in living cells, but less is known about their roles in the development process and the functional network with other factors. Here, we show that Arabidopsis (Arabidopsis thaliana) JACALIN-LECTIN LIKE1 (AtJAC1) functions in flowering time control. Loss of function of AtJAC1 leads to precocious flowering, whereas overexpression of AtJAC1 causes delayed flowering. AtJAC1 influences flowering through regulation of the key flowering repressor gene FLOWERING LOCUS C (FLC). Genetic analysis revealed that AtJAC1's function is mostly dependent on GLYCINE-RICH RNA-BINDING PROTEIN7 (GRP7), an upstream regulator of FLC. Biochemical and cell biological data indicated that AtJAC1 interacted physically with GRP7 specifically in the cytoplasm. AtJAC1 influences the nucleocytoplasmic distribution of GRP7, with predominant nuclear localization of GRP7 when AtJAC1 function is lost but retention of GRP7 in the cytoplasm when AtJAC1 is overexpressed. A temporal inducible assay suggested that AtJAC1's regulation of flowering could be compromised by the nuclear accumulation of GRP7. In addition, GRP7 binds to the antisense precursor messenger RNA of FLC through a conserved RNA motif. Loss of GRP7 function leads to the elevation of total FLC antisense transcripts and reduced proximal-distal polyadenylation ratio, as well as histone methylation changes in the FLC gene body region and increased total functional sense FLC transcript. Attenuating the direct binding of GRP7 with competing artificial RNAs leads to changes of FLC antisense precursor messenger RNA processing and flowering transition. Taken together, our study indicates that AtJAC1 coordinates with GRP7 in shaping plant development through the regulation of RNA processing in Arabidopsis.

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“…Like the inducible lectins (Lannoo and Van Damme, 2010), AtJAC1 is a nucleocytoplasmic protein (Supplemental Fig. S4A).…”

Section: Jacalin-lectins Interact With Rna-binding Proteins and Regulmentioning

confidence: 99%

Section: Grp7bsmentioning

confidence: 99%

AtJAC1 Regulates Nuclear Accumulation of GRP7, Influencing RNA Processing of FLC Antisense Transcripts and Flowering Time in Arabidopsis

Xiao

et al. 2015

Plant Physiol.

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“…Since the expression of most of these lectins is up-regulated by various (a)biotic stress factors, it was hypothesized that these lectins fulfill a role in cellular signaling events in response to stress conditions (Lannoo and Van Damme, 2010). Hitherto, the physiological role of none of these proteins was investigated.…”

Section: Resultsmentioning

confidence: 99%

“…Since the expression of several nucleocytoplasmic lectins was shown to be inducible by (a)biotic stress factors (Claes et al, 1990;Van Damme, 2008;Fouquaert et al, 2009;Vandenborre et al, 2009), these lectins are believed to be involved in stress signaling (Van Damme et al, 2004, Van Damme, 2008. However, until now, this hypothesis has awaited confirmation, since no putative receptors have been identified for nucleocytoplasmic plant lectins (Lannoo and Van Damme, 2010).…”

mentioning

confidence: 96%

“…Further localization studies have shown that this group of lectins locates to the nuclear and/or cytoplasmic compartment of the plant cell. According to their subcellular localization, these lectins were called nucleocytoplasmic plant lectins (Lannoo and Van Damme, 2010). Since the expression of several nucleocytoplasmic lectins was shown to be inducible by (a)biotic stress factors (Claes et al, 1990;Van Damme, 2008;Fouquaert et al, 2009;Vandenborre et al, 2009), these lectins are believed to be involved in stress signaling (Van Damme et al, 2004, Van Damme, 2008.…”

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confidence: 99%

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Interaction of the Tobacco Lectin with Histone Proteins

et al. 2011

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The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells. Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant. In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells. Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins. Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column. Elution of Nictaba-interacting histone proteins was achieved with 1 M N-acetylglucosamine (GlcNAc). Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc. Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.

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History of Plant Lectin Research

Damme

2014

Methods in Molecular Biology

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Numerous plant species are known to express one or more lectins or proteins containing a lectin domain, enabling these proteins to select and bind specific carbohydrate structures. The group of plant lectins is quite heterogeneous since lectins differ in their molecular structure, specificity for certain carbohydrate structures, and biological activities resulting therefrom. This chapter presents a short historical overview on how plant lectin research has evolved over the years from a discipline aiming merely at the purification and characterization of plant lectins towards the application of plant lectins as tools in glycobiology.

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Nucleocytoplasmic plant lectins

Cited by 111 publications

References 151 publications

AtJAC1 Regulates Nuclear Accumulation of GRP7, Influencing RNA Processing of FLC Antisense Transcripts and Flowering Time in Arabidopsis

AtJAC1 Regulates Nuclear Accumulation of GRP7, Influencing RNA Processing of FLC Antisense Transcripts and Flowering Time in Arabidopsis

Interaction of the Tobacco Lectin with Histone Proteins

History of Plant Lectin Research

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