Ion dependence of the discoidin I lectin from Dictyostelium discoideum

Alexander, Stephen; Cibulsky, A M; Lerner, Richard A.

doi:10.1111/j.1432-0436.1983.tb01321.x

Cited by 16 publications

(8 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Both mutant JH104 and wild-type AX2 cells were grown in either fresh suspensions of K. aerogenes or in cultures prepared with buffer previously conditioned by AX2 cells and known to contain PSF. [2][3][4][5]. 6, both strains responded to conditioned buffer and expressed the discoidin I genes.…”

Section: Although the Adjacent Lane To The Left (Not Shown) Was Ovementioning

confidence: 92%

Multiple signal transduction pathways regulate discoidin I gene expression in Dictyostelium discoideum

1995

Self Cite

View full text Add to dashboard Cite

Section: Although the Adjacent Lane To The Left (Not Shown) Was Ovementioning

confidence: 92%

Multiple signal transduction pathways regulate discoidin I gene expression in Dictyostelium discoideum

1995

Self Cite

View full text Add to dashboard Cite

“…All of the gene products bind to galactose (23). The binding of the discoidin I molecules is Ca2+ dependent (2).…”

mentioning

confidence: 99%

Translational control of discoidin lectin expression in drsA suppressor mutants of Dictyostelium discoideum.

Alexander¹,

Leone²,

Ostermeyer³

1991

Mol. Cell. Biol.

View full text Add to dashboard Cite

Genetic analysis in Dictyostelium discoideum has identified regulatory genes which control the developmental expression of the discoidin lectin multigene family. Among these, the drsA mutation is a dominant second-site suppressor of another mutation, disB, which has the discoidinless phenotype. We now demonstrate a novel mechanism by which the drsA allele exerts its suppressive effect on the disB mutation. Interestingly, drsA does not merely bypass the disB mutation and restore the wild-type pattern of lectin expression. Rather, drsA mutant cells have high levels of discoidin lectin synthesis during growth but do not express lectins during aggregation. In contrast, wild-type cells only express lectin protein during the aggregation period of development. Phenocopies of the drsA mutation show a pattern of discoidin expression similar to that seen in the bona fide mutant. These data suggest that there may be a mechanism of negative feedback, resulting from the high levels of discoidin lectin made during growth, which inhibits further discoidin lectin expression during development. Northern (RNA) analysis of developing drsA mutant cells shows that these cells contain high levels of discoidin mRNA, although no discoidin lectin protein is being translated from these messages. Therefore, expression of the discoidin gene family can be controlled at the level of translation as well as transcription.

show abstract

“…The interactions that involve four β-strands over six would help to maintain the trimeric arrangement of the lectin domain. That would explain the dependence for divalent cation for carbohydrate binding and the destabilising role of EDTA and EGTA observed for DiscI 28. In DiscII, which is not calcium-dependant, the position of the calcium ion is occupied by the NZ of Lys206 and other interactions stabilise the trimer.…”

Section: Resultsmentioning

confidence: 93%

“…DiscI also recognises glycoconjugates that contain GalNAc in the slime coat around aggregates and in multilamellar bodies since the interaction is completely blocked in the presence of GalNAc 25,26,27. The sugar binding site was shown to be different of the cell adhesion site and requires a divalent cation 24,28…”

Section: Introductionmentioning

confidence: 99%

Discoidin I from Dictyostelium discoideum and Interactions with Oligosaccharides: Specificity, Affinity, Crystal Structures, and Comparison with Discoidin II

Mathieu

Aragão

Imberty

et al. 2010

Journal of Molecular Biology

View full text Add to dashboard Cite

Discoidin I and Discoidin II (DiscI and DiscII), are N-acetylgalactosamine-binding proteins from Dictyostelium discoideum. They consist of two domains with an N-terminal discoidin domain and a C-terminal H-type lectin domain. They were cloned and expressed in high yield in recombinant form in Escherichia coli. Although both lectins bind galactose and N-acetylgalactosamine, glycan array experiments performed on the recombinant proteins displayed strong differences in their specificity for oligosaccharides. DiscI and DiscII bind preferentially to Gal/GalNAcβ1-3Gal/ GalNAc-and Gal/GalNAcβ1-4GlcNAcβ1-6Gal/GalNAc-containing glycans respectively. The affinity of the interaction of DiscI with monosaccharides and disaccharides was evaluated using isothermal calorimetry experiments. The tree-dimensional structures of native DiscI and its complexes with GalNAc, GalNAcβ1-3Gal and Galβ1-3GalNAc were solved by X-ray crystallography. DiscI forms trimers with involvement of calcium at the monomer interface. The N-terminal discoidin domain presents structural similarity to F-type lectins such as the eel agglutinin where an amphiphilic binding pocket suggests a possible carbohydrate-binding activity. In the C-terminal H-type lectin domain, the GalNAc residue establishes specific hydrogen bonds that explain the observed affinity (K d = 3 10 -4 M). The different specificities of DiscI and DiscII for oligosaccharides were rationalized from the different structures obtained by either X-ray crystallography or molecular modelling.

show abstract

Ion dependence of the discoidin I lectin from Dictyostelium discoideum

Cited by 16 publications

References 20 publications

Multiple signal transduction pathways regulate discoidin I gene expression in Dictyostelium discoideum

Multiple signal transduction pathways regulate discoidin I gene expression in Dictyostelium discoideum

Translational control of discoidin lectin expression in drsA suppressor mutants of Dictyostelium discoideum.

Discoidin I from Dictyostelium discoideum and Interactions with Oligosaccharides: Specificity, Affinity, Crystal Structures, and Comparison with Discoidin II

Contact Info

Product

Resources

About