Sequence and expression of Thai Rosewood beta-glucosidase/beta-fucosidase, a family 1 glycosyl hydrolase glycoprotein.

Dalcochinin-8'-O-beta-glucoside beta-glucosidase (dalcochinase) from the Thai rosewood (Dalbergia cochinchinensis Pierre) has aglycone specificity for isoflavonoids and can hydrolyze both beta-glucosides and beta-fucosides. To determine its structure and evolutionary lineage, the sequence of the enzyme was determined by peptide sequencing followed by PCR cloning. The cDNA included a reading frame coding for 547 amino acids including a 23 amino acid propeptide and a 524 amino acid mature protein.

Apoptosis-induced cleavage of beta-catenin by caspase-3 results in proteolytic fragments with reduced transactivation potential.

Beta-catenin is a member of the Armadillo repeat protein family with a dual cellular function as a component of both the adherens junction complex and the Wnt/wingless signaling pathway. Here we show that beta-catenin is proteolytically cleaved during anoikis and staurosporine-induced apoptosis. Cleavage of beta-catenin was found to be caspase-dependent.

The relationship of certain tymoviruses assessed from the amino acid composition of their coat proteins.

The amino acid composition of the coat proteins of the following viruses is reported: Andean potato latent, clitoria yellow vein, desmodium yellow mottle, dulcamara mottle, eggplant mosaic, okra mosaic, ononis yellow mosaic, scrophularia mottle, and, as controls, cocksfoot mild mosaic and cocksfoot mottle viruses. These data, together with some already published, were used to compute classifications of the tymoviruses. These classifications show a general similarity to Koenig's serological classification of the tymoviruses, but the correlation is poor, unlike similar comparisons of tobamovirus classifications.