Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family

Hester, G.; Kaku, Hanae; Goldstein, Irwin J.; Wright, Christopher S.

doi:10.1038/nsb0695-472

Cited by 195 publications

(200 citation statements)

References 31 publications

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“…2 A). Each of these domains consists of a 12-stranded ␤-prism II fold similar to that reported in other single-domain mannose-binding lectins (15)(16)(17), although LLD1 and LLD2 share only 18% amino acid sequence identity compared with 55% identity between the two lectin-like domains of SCAfet (18). In support of this predicted structure, the region linking LLD1 and LLD2 corresponds to a ''deletable region'' previously identified (18) from sequence alignments of various SRK variants ( Fig.…”

Section: Identification Of Structural Modules Within Esrk By Homologymentioning

confidence: 92%

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

Naithani¹,

Chookajorn²,

Ripoll

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

109

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The highly polymorphic S-locus receptor kinase (SRK) is the stigma determinant of specificity in the self-incompatibility response of the Brassicaceae. SRK spans the plasma membrane of stigma epidermal cells, and it is activated in an allele-specific manner on binding of its extracellular region (eSRK) to its cognate pollen coat-localized S-locus cysteine-rich (SCR) ligand. SRK, like several other receptor kinases, forms dimers in the absence of ligand. To identify domains in SRK that mediate ligand-independent dimerization, we assayed eSRK for self-interaction in yeast. We show that SRK dimerization is mediated by two regions in eSRK, primarily by a C-terminal region inferred by homology modeling/fold recognition techniques to assume a PAN APPLE-like structure, and secondarily by a region containing a signature sequence of the S-domain gene family, which might assume an EGF-like structure. We also show that eSRK exhibits a marked preference for homodimerization over heterodimerization with other eSRK variants and that this preference is mediated by a small, highly variable region within the PAN APPLE domain. Thus, the extensive polymorphism exhibited by the eSRK not only determines differential affinity toward the SCR ligand, as has been assumed thus far, but also underlies a previously unrecognized allelic specificity in SRK dimerization. We propose that preference for SRK homodimerization explains the codominance exhibited by a majority of SRKs in the typically heterozygous stigmas of self-incompatible plants, whereas an increased propensity for heterodimerization combined with reduced affinity of heterodimers for cognate SCRs might underlie the dominant-recessive or mutual weakening relationships exhibited by some SRK allelic pairs.self-incompatibility ͉ ligand-independent receptor dimerization ͉ yeast two-hybrid T he S-locus receptor kinase (SRK) is a single-pass integral plasma membrane protein of the stigma epidermis that functions in the recognition and rejection of self-related pollen in self-incompatible members of the Brassicaceae (reviewed in refs. 1 and 2). The SRK receptor and its pollen-coat localized ligand, the S-locus cysteine-rich protein (SCR) (1), also designated SP-11 (2), are encoded by tightly linked and highly polymorphic genes within the S-locus haplotype. Specificity in the self-incompatibility response derives from allele-specific SRK-SCR interaction (3, 4). On self-pollination, the binding of SCR to the extracellular domain of its cognate SRK activates the receptor and triggers an intracellular signaling cascade that leads to arrest of ''self'' pollen tubes. In contrast, pollen tube growth in cross-pollinations proceeds unimpeded because ''nonself'' SCR cannot bind SRK. In view of this high degree of specificity in the affinity of SRK for its SCR ligand, the extensive polymorphisms exhibited by the SRK extracellular region (eSRK) have heretofore been considered in the context of specificity in the SRK-SCR interaction.The eSRK does more than interact with SCR, however. SRK forms oligo...

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Section: Identification Of Structural Modules Within Esrk By Homologymentioning

confidence: 92%

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

Naithani¹,

Chookajorn²,

Ripoll

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

109

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“…Recently the three-dimensional structure of GNA was elucidated and its binding site for ␣-methyl mannoside in each monomer was identified (22). With regard to molecular structure, CVA also is a tetrameric protein with similar molecular size and amino acid composition as that of GNA.…”

Section: ␣-13-mannosylmannose Recognizing Lectinmentioning

confidence: 99%

“…It is possible that acidic residue(s) are involved in the carbohydrate-binding site of CVA inasmuch as the ascending portion of the pH profile (pK ϭ ϳ3.5-4.0) is in the titration range of ␤-and ␥-carboxyl groups of Asp and Glu. Acidic amino acid residues have been identified in many lectinbinding sites including the snowdrop lectin (22).…”

Section: ␣-13-mannosylmannose Recognizing Lectinmentioning

confidence: 99%

Purification and Characterization of the α-1,3-Mannosylmannose-recognizing Lectin of Crocus vernusBulbs

Misaki

Kakuta

Meah

et al. 1997

Journal of Biological Chemistry

Self Cite

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A unique mannose-binding lectin, highly specific for terminal Man(␣1,3)Man groups, was isolated from bulbs of crocus (Crocus vernus All.). The lectin failed to bind to a mannose affinity column and was purified by simple gel permeation chromatography (Sephacryl S200). The purified lectin, obtained in crystalline form, had a molecular mass of 44 kDa on gel filtration and showed a single peptide band with a molecular mass of 11 kDa on SDS-polyacrylamide gel electrophoresis, indicating it to be a tetrameric protein composed of four identical subunits. The N-terminal amino acid sequence analysis of the crocus lectin showed essentially no homology with that of other mannose-binding bulb lectins. The crocus lectin selectively interacted with the wild type Saccharomyces cerevisiae and other mannans carrying terminal Man(␣1,3)Man but not with those lacking this disaccharide unit. In hapten inhibition studies, methyl ␣-mannopyranoside did not inhibit the mannan-lectin interaction. Of various ␣-mannooligosaccharides, those having the Man(␣1,3)Man sequence showed the highest inhibitory potency, confirming the strict requirement of lectin for terminal ␣1,3-linked mannosylmannose units. An affinity column of immobilized lectin enabled the complete resolution of yeast mannan and glycogen. The immobilized lectin may provide a useful tool for purification and analysis of biologically important polysaccharides and glycoproteins.Since the first report on a yeast mannan-binding lectin from bulbs of tulip, Tulipa generiana (1), several kinds of ␣-mannose-binding lectins have been studied in our laboratory, mostly from bulbs of the family Amaryllidaceae, such as Galanthus nivalis (snow drop; GNA) 1 (2, 3), Hippeastrum hybrid (amaryllis), Narcissus pseudonarcissus (daffodil) (4), Sternbergia lutea (5), and Allium sativum (garlic) (6), which belongs to the Lilaceae family. A similar lectin was also isolated from leaves of Listera ovata (twayblade) (7). These lectins are distinct from hitherto known mannose/glucose-binding lectins, such as concanavalin A and other legume lectins, in their strict requirement for the axial C-2 hydroxyl group of ␣-D-mannopyranose. Our detailed studies of the carbohydrate binding specificity of these lectins have indicated some differences with regard to the location of mannosidic linkages at the terminal and/or internal position in the carbohydrate chain. For instance, GNA recognizes terminal Man(␣1,3)Man (3) and also certain internal linkages (8). Similarly, L. ovata lectin can recognize the internal sequence of ␣(1,3)-linked mannosidic linkages (7). In a survey of new plant lectins we found that the bulbs of Crocus vernus All., belonging to the family Iridaceae, accumulates a very unique mannose-binding lectin with a very strict requirement for terminal ␣-1,3-mannosyl mannose units. This lectin, designated CVA, agglutinates rabbit but not human erythrocytes and does not appear to have homology with hitherto known mannose-binding lectins in its sequence of Nterminal amino acids. This paper reports the pu...

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“…More recently, the structures of lectins from snowdrop and amaryllis bulbs were determined (Hester, Kaku, Goldstein & Wright, 1995;Chantalat, Wood, Rizkallah & Reynolds, 1996) and shown to contain a new class of protein fold consisting of three antiparallel four-stranded fl-sheets arranged as a 12-stranded fl-barrel.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray analysis of a novel plant lectin from Calystegia sepium

Wright¹,

Wood²,

Reynolds³

et al. 1997

Acta Cryst D

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A mannose-specific lectin from Calystegia sepium has been crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The needle-shaped crystals are orthorhombic, space group C222~ with cell dimensions a = 55.2(1), b= 55.9 (1), c = 196.1 (1)A. Fresh crystals diffract to 1.9 A resolution on a synchrotron radiation source. The asymmetric unit contains a dimer of two identical 16 kDa subunits with a packing density of 2.36 ~3 Da-1. Intensity data have been observed beyond 2.0~, but reasonable statistics restricted the usable range to 2.0 A.

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Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family

Cited by 195 publications

References 31 publications

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

Purification and Characterization of the α-1,3-Mannosylmannose-recognizing Lectin of Crocus vernusBulbs

Crystallization and preliminary X-ray analysis of a novel plant lectin from Calystegia sepium

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