Enzymatic activity of Cyathus olla during solid state fermentation of canola roots

Le Cyathus olla, une nidulaire, est étudié comme agent de lutte biologique contre les maladies du canola véhiculées par le chaume. Dans cette étude, notre but est de détecter et d'identifier des enzymes produites par le C. olla lors de la fermentation, en milieu solide, de racines de canola et capables de dégrader les parois cellulaires de plantes. Nous avons trouvé des activités laccase et manganèse peroxydase après 1 et 4 semaines d'incubation, et une activité aryl alcool oxydase après 4 semaines d'incubation. Des extraits bruts dans du tampon ont été testés pour la présence de cellulases et de polygalacturonase, mais seulement la polygalacturonase a été détectée. Nous en concluons que le C. olla possède des enzymes pour dégrader la lignine et qu'il pourrait être utilisé comme inoculant pour accélérer la décomposition du chaume.Cyathus olla, a bird's nest fungus, is being studied as a biological control agent of stubble-borne diseases of canola. Our objectives in this study were to detect and identify plant cell wall degrading enzymes produced by C. olla during solid state fermentation of canola roots. We identified laccase and manganese peroxidase in both 1- and 4-week incubations, and aryl-alcohol oxidase was detected following 4 weeks of incubation. Crude buffer extracts were assayed for cellulases and polygalacturonase, but only the latter was detected. We conclude that C. olla has enzymes to degrade lignin and that it may have use as an inoculant to accelerate stubble decomposition

Phasic Phosphorylation of Caldesmon and ERK 1/2 during Contractions in Human Myometrium

Human myometrium develops phasic contractions during labor. Phosphorylation of caldesmon (h-CaD) and extracellular signal-regulated kinase 1/2 (ERK 1/2) has been implicated in development of these contractions, however the phospho-regulation of these proteins is yet to be examined during periods of both contraction and relaxation. We hypothesized that protein phosphorylation events are implicated in the phasic nature of myometrial contractions, and aimed to examine h-CaD and ERK 1/2 phosphorylation in myometrium snap frozen at specific stages, including; (1) prior to onset of contractions, (2) at peak contraction and (3) during relaxation. We aimed to compare h-CaD and ERK 1/2 phosphorylation in vitro against results from in vivo studies that compared not-in-labor (NIL) and laboring (L) myometrium. Comparison of NIL (n = 8) and L (n = 8) myometrium revealed a 2-fold increase in h-CaD phosphorylation (ser-789; P = 0.012) during onset of labor in vivo, and was associated with significantly up-regulated ERK2 expression (P = 0.022), however no change in ERK2 phosphorylation was observed (P = 0.475). During in vitro studies (n = 5), transition from non-contracting tissue to tissue at peak contraction was associated with increased phosphorylation of both h-CaD and ERK 1/2. Furthermore, tissue preserved at relaxation phase exhibited diminished levels of h-CaD and ERK 1/2 phosphorylation compared to tissue preserved at peak contraction, thereby producing a phasic phosphorylation profile for h-CaD and ERK 1/2. h-CaD and ERK 1/2 are phosphorylated during myometrial contractions, however their phospho-regulation is dynamic, in that h-CaD and ERK 1/2 are phosphorylated and dephosphorylated in phase with contraction and relaxation respectively. Comparisons of NIL and L tissue are at risk of failing to detect these changes, as L samples are not necessarily preserved in the midst of an active contraction

The structure basis for specificity in human ABO(H) blood group biosynthesis: Nature Struc.Biol.

NRC publication: Ye

Crystallization of the recombinant human blood group A and B glycosyltransferase

NRC publication: Ye