Interaction of a novel cysteine and histidine‐rich cytoplasmic protein with galectin‐3 in a carbohydrate‐independent manner

FEBS Letters

Hughes, R.Colin¹  Menon, Rajesh P.¹  Strom, Molly¹ 

[1] Divisions of Protein Structure and Membrane Biology, National Institute for Medical Research, Mill Hill, London NW7 1AA, UK

关键词: Galectin-3;    Two-hybrid screen;    Novel protein;   

DOI  :  10.1016/S0014-5793(00)01310-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have used the yeast two-hybrid system to search for cytoplasmic proteins that might assist in the intracellular trafficking of the soluble β-galactoside-binding protein, galectin-3. We utilised as bait murine full-length galectin-3 to screen a murine 3T3 cDNA library. Several interacting clones were found to encode a partial open reading frame and a full-length clone was obtained by rapid amplification of cDNA ends methodology. In various assays in vitro the novel protein was shown to bind galectin-3 in a carbohydrate-independent manner. The novel protein contains an unusually high content of cysteine and histidine residues and shows significant sequence homologies with several metal ion-binding motifs present in known proteins. Confocal immunofluorescence microscopy of permeabilised 3T3 cells shows a prominent perinuclear, as well as cytoplasmic, localisation of the novel protein.

【 授权许可】

Unknown