Arabidopsis F‐box protein containing a Nictaba‐related lectin domain interacts with <i>N</i>‐acetyllactosamine structures

Stefanowicz, Karolina; Lannoo, Nausicaä; Proost, Paul; Damme, Els J.M. Van

doi:10.1016/j.fob.2012.06.002

Cited by 31 publications

(23 citation statements)

References 39 publications

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“…2012; Stefanowicz et al, 2012). Further studies are necessary to elucidate the carbohydrate-binding specificities of NLL proteins in other species.…”

Section: Discussionmentioning

confidence: 99%

Evolution and structural diversification ofNictaba-like lectin genes in food crops with a focus on soybean (Glycine max)

Holle¹,

Rougé²,

Damme³

2017

Ann Bot

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Background and Aims The Nictaba family groups all proteins that show homology to Nictaba, the tobacco lectin. So far, Nictaba and an Arabidopsis thaliana homologue have been shown to be implicated in the plant stress response. The availability of more than 50 sequenced plant genomes provided the opportunity for a genome-wide identification of Nictaba-like genes in 15 species, representing members of the Fabaceae, Poaceae, Solanaceae, Musaceae, Arecaceae, Malvaceae and Rubiaceae. Additionally, phylogenetic relationships between the different species were explored. Furthermore, this study included domain organization analysis, searching for orthologous genes in the legume family and transcript profiling of the Nictaba-like lectin genes in soybean.Methods Using a combination of BLASTp, InterPro analysis and hidden Markov models, the genomes of Medicago truncatula, Cicer arietinum, Lotus japonicus, Glycine max, Cajanus cajan, Phaseolus vulgaris, Theobroma cacao, Solanum lycopersicum, Solanum tuberosum, Coffea canephora, Oryza sativa, Zea mays, Sorghum bicolor, Musa acuminata and Elaeis guineensis were searched for Nictaba-like genes. Phylogenetic analysis was performed using RAxML and additional protein domains in the Nictaba-like sequences were identified using InterPro. Expression analysis of the soybean Nictaba-like genes was investigated using microarray data.Key Results Nictaba-like genes were identified in all studied species and analysis of the duplication events demonstrated that both tandem and segmental duplication contributed to the expansion of the Nictaba gene family in angiosperms. The single-domain Nictaba protein and the multi-domain F-box Nictaba architectures are ubiquitous among all analysed species and microarray analysis revealed differential expression patterns for all soybean Nictaba-like genes.Conclusions Taken together, the comparative genomics data contributes to our understanding of the Nictaba-like gene family in species for which the occurrence of Nictaba domains had not yet been investigated. Given the ubiquitous nature of these genes, they have probably acquired new functions over time and are expected to take on various roles in plant development and defence.

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“…2012; Stefanowicz et al, 2012). Further studies are necessary to elucidate the carbohydrate-binding specificities of NLL proteins in other species.…”

Section: Discussionmentioning

confidence: 99%

Evolution and structural diversification ofNictaba-like lectin genes in food crops with a focus on soybean (Glycine max)

Holle¹,

Rougé²,

Damme³

2017

Ann Bot

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“…Clearly, these possibilities are not mutually exclusive and perhaps occur in parallel. Interestingly, some F-box proteins containing a lectinlike domain can bind to various carbohydrate epitopes including core a1,3-fucose, implying a role for complex N-glycans in protein turnover (Stefanowicz et al, 2012). In addition, a recent report showed that KOR1 is part of the cellulose synthase complex required for normal motility and intracellular trafficking of the CSC (Vain et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Multiple N-Glycans Cooperate in the Subcellular Targeting and Functioning of Arabidopsis KORRIGAN1

et al. 2014

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Arabidopsis thaliana KORRIGAN1 (KOR1) is an integral membrane endo-b1,4-glucanase in the trans-Golgi network and plasma membrane that is essential for cellulose biosynthesis. The extracellular domain of KOR1 contains eight N-glycosylation sites, N1 to N8, of which only N3 to N7 are highly conserved. Genetic evidence indicated that cellular defects in attachment and maturation of these N-glycans affect KOR1 function in vivo, whereas the manner by which N-glycans modulate KOR1 function remained obscure. Site-directed mutagenesis analysis of green fluorescent protein (GFP)-KOR1 expressed from its native regulatory sequences established that all eight N-glycosylation sites (N1 to N8) are used in the wild type, whereas stt3a-2 cells could only inefficiently add N-glycans to less conserved sites. GFP-KOR1 variants with a single N-glycan at nonconserved sites were less effective than those with one at a highly conserved site in rescuing the root growth phenotype of rsw2-1 (kor1 allele). When functionally compromised, GFP-KOR1 tended to accumulate at the tonoplast. GFP-KOR1Dall (without any N-glycan) exhibited partial complementation of rsw2-1; however, root growth of this line was still negatively affected by the absence of complex-type N-glycan modifications in the host plants. These results suggest that one or several additional factor(s) carrying complex N-glycans cooperate(s) with KOR1 in trans to grant proper targeting/functioning in plant cells.

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“…Glycan array analyses revealed the F-box protein encoded by At2g02360 exhibits carbohydrate binding activity toward N - and O -glycans with N -acetyllactosamine (LacNAc; Galβ1–3GlcNAc and Galβ1–4GlcNAc) and poly-LacNAc structures as well as with Lewis A (Galβ1–3(Fucα1–4)GlcNAc), Lewis X (Galβ1–4(Fuca1–3)GlcNAc), Lewis Y (Fucα1–2Galβ1–4(Fucα1–3)GlcNAc), and type-1 B motifs (Galα1–3(Fucα1–2)Galβ1–3GlcNAc. Since these glycan structures have been reported in bacteria, viruses, and animals rather than in plants the physiological importance of this glycan interaction remains enigmatic (Lannoo et al, 2008; Stefanowicz et al, 2012). Furthermore, the same Arabidopsis F-box Nictaba protein was shown to interact with core members of an E3-type ubiquitin ligase complex which resulted in the hypothesis assuming a role of the Nictaba domain in glycoprotein degradation (Takahashi et al, 2004; Arabidopsis Interactome Mapping Consortium, 2011).…”

Section: Pathogen Recognition Based On Protein–carbohydrate Interactionsmentioning

confidence: 99%

Lectin domains at the frontiers of plant defense

2014

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Plants are under constant attack from pathogens and herbivorous insects. To protect and defend themselves, plants evolved a multi-layered surveillance system, known as the innate immune system. Plants sense their encounters upon perception of conserved microbial structures and damage-associated patterns using cell-surface and intracellular immune receptors. Plant lectins and proteins with one or more lectin domains represent a major part of these receptors. The whole group of plant lectins comprises an elaborate collection of proteins capable of recognizing and interacting with specific carbohydrate structures, either originating from the invading organisms or from damaged plant cell wall structures. Due to the vast diversity in protein structures, carbohydrate recognition domains and glycan binding specificities, plant lectins constitute a very diverse protein superfamily. In the last decade, new types of nucleocytoplasmic plant lectins have been identified and characterized, in particular lectins expressed inside the nucleus and the cytoplasm of plant cells often as part of a specific plant response upon exposure to different stress factors or changing environmental conditions. In this review, we provide an overview on plant lectin motifs used in the constant battle against pathogens and predators during plant defenses.

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Arabidopsis F‐box protein containing a Nictaba‐related lectin domain interacts with N‐acetyllactosamine structures

Abstract: Highlights► Recombinant expression of a new type of Arabidopsis F-box protein. ► Arabidopsis F-box-Nictaba protein is a functional lectin. ► Arabidopsis F-box-Nictaba recognizes N-acetyllactosamine and Lewis structures.

Cited by 31 publications

References 39 publications

Evolution and structural diversification ofNictaba-like lectin genes in food crops with a focus on soybean (Glycine max)

Evolution and structural diversification ofNictaba-like lectin genes in food crops with a focus on soybean (Glycine max)

Multiple N-Glycans Cooperate in the Subcellular Targeting and Functioning of Arabidopsis KORRIGAN1

Lectin domains at the frontiers of plant defense

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