Guanosine diphosphate-L-fucose glycopeptide fucosyltransferase activity in Corynebacterium insidiosum.

The biosynthesis of a phytotoxic glycopeptide of Corynebacterium insidiosum involves guanosine diphosphate-l-fucosyltransferase activity. This enzyme activity is most consistently associated with the cellular membranes fraction. The optimal pH for the transfer reaction is 7.

Biochemical basis of the resistance of sugarcane to eyespot disease.

Helminthosporoside is the host-specific toxin produced by Helminthosporium sacchari, the organism causing eyespot disease on sugarcane. Clones of sugarcane susceptible to the toxin posses a membrane protein that binds the toxin. Membranes of resistant clones do not bind the toxin.

A Phytotoxic Glycopeptide from Cultures of Corynebacterium insidiosum.

Cultures of Corynebacterium insidiosum produce an extra-cellular phytotoxic glycopeptide that possesses the ability to wilt plant cuttings. Wilt induced by this glycopeptide is directly dependent upon time and upon concentration with measureable wilt occurring in 40 nm solutions in 1 hour. The organism produces 1.

Adenosine Diphosphate-Glucose Pyrophosphorylase Control of Starch Accumulation in Rust-infected Wheat Leaves.

The variation in starch content in healthy and Puccinia striiformsi-infected wheat leaves was measured from 5 to 15 days after inoculation. The starch content of diseased leaves relative to healthy leaves decreased from 5 to 9 days, increased from 9 to 12 days to twice that of healthy leaves, and decreased from 12 to 15 days after inoculation. Electron micrographs of plant tissues indicated that the starch accumulated in the chloroplasts of host cells adjacent to fungal hyphae.

The Active Site on the Phytotoxin of Corynebacterium sepedonicum.

Corynebacterium sepedonicum produces an extracellular phytotoxic glycopeptide that possesses a capacity to wilt plant cuttings. It has been previously demonstrated that the integrity of some of the membranes of the host cells is destroyed, suggesting the possibility that a biologically active site is present on the toxin molecule. The toxin was chemically altered in the following ways and then tested for biological activity: (a) the NH(2)-terminal group on the peptide portion of the toxin was blocked by the dansylation technique; (b) the OH groups on the sugar and amino acid residues as well as the NH groups on the amino acid residues were blocked by exhaustive methylation; (c) the COO(-) groups were converted to their respective methyl esters; (d) the peptide moiety was removed by pronase digestion.