Didemnin B: Comparative study and conformational approach in solution

A comparative study of isodideimnine-1 and didemnin B is presented using spcctroecopic methods, partial degradation and partial synthesis. This leads to the conclusion of the presence of a single depsipeptide, namely didemnin B, with (3S,4R,5S) isostatine instead of the previous statine residue. An attempt to determine the whole conformation in solution of didemnin B by using 2D-NMR is also described

Hb Mont Saint Aignan [beta 128(H6)Ala -> Pro]: A new unstable variant leading to chronic microcytic anemia

Hb Mont Saint-Aignan [beta 128(H6)Ala –> Pro] is a mildly unstable variant, associated with hemolytic anemia, marked microcytosis and increased alp biosynthetic ratio (1.55 versus 1.1 +/-0.1 in the control). The abnormal chain was isolated by selective precipitation with isopropanol and the structural modification determined by protein chemistry methods (reversed phase high performance liquid chromatography and mass spectrometry). Possible mechanisms underlying the beta (+)-thalassemia-like expression of this variant are discussed

Rhizobium sp. strain NGR234 NodZ protein is a fucosyltransferase.

Rhizobium sp. strain NGR234 produces a large family of lipochitooligosaccharide Nod factors carrying specific substituents. Among them are 3-O- (or 4-O-) and 6-O-carbamoyl groups, an N-methyl group, and a 2-O-methylfucose residue which may bear either 3-O-sulfate or 4-O-acetyl substitutions. Investigations on the genetic control of host specificity revealed a number of loci which directly affect Nod factor structure. Here we show that insertion and frameshift mutations in the nodZ gene abolish fucosylation of Nod factors. In vitro assays using GDP-L-fucose as the fucose donor show that fucosyltransferase activity is associated with the nodZ gene product (NodZ). NodZ is located in the soluble protein fraction of NGR234 cells. Together with extra copies of the nodD1 gene, the nodZ gene and its associated nod box were introduced into ANU265, which is NGR234 cured of the symbiotic plasmid. Crude extracts of this transconjugant possess fucosyltransferase activity. Fusion of a His6 tag to the NodZ protein expressed in Escherichia coli yielded a protein able to fucosylate both nonfucosylated NodNGR factors and oligomers of chitin. NodZ is inactive on monomeric N-acetyl-D-glucosamine and on desulfated Rhizobium meliloti Nod factors. Kinetic analyses showed that the NodZ protein is more active on oligomers of chitin than on nonfucosylated NodNGR factors. Pentameric chitin is the preferred substrate. These data suggest that fucosylation occurs before acylation of the Nod factors