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Evidence For An Epigenetic Mechanism By Which Hsp90 Acts As A Capacitor For Morphological Evolution, Vincent E. Sollars, Xiangyi Lu, Li Xiao, Xiaoyan Wang, Mark D. Garfinkel, Douglas M. Ruden

Vincent E Sollars

Morphological alterations have been shown to occur in Drosophila melanogaster when function of Hsp90 (heat shock 0-kDa protein 1α, encoded by Hsp83) is compromised during development1. Genetic selection maintains the altered phenotypes in subsequent generations1. Recent experiments have shown, however, that phenotypic variation still occurs in nearly isogenic recombinant inbred strains of Arabidopsis thaliana2. Using a sensitized isogenic D. melanogaster strain, iso-KrIf-1, we confirm this finding and present evidence supporting an epigenetic mechanism for Hsp90’s capacitor function, whereby reduced activity of Hsp90 induces a heritably altered chromatin state. The altered chromatin state is evidenced by ectopic expression of the morphogen …

Genetics And Biochemistry Of Protein Glycosylation In Campylobacter Jejuni, Alexandra Merkx-Jacques, S. Vijayakumar, M. Demendi, D. Ratnayake, C. Dozois, C. Creuzenet

Alexandra Merkx-Jacques

BACKGROUND: C. jejuni produces numerous glycoproteins, including flagellins, which are important for virulence. The flagellins harbour pseudaminic acid (PA) whereas other glycoproteins harbour diacetamidobacillosamine (DAB). We are investigating the genetics and biochemistry of protein glycosylation in C. jejuni to identify the enzymes involved, and determine their activity and roles in virulence. We focused on two homologous pathways comprising each a putative dehydratase, aminotransferase and acetyltransferase, namely {Cj1293, Cj1294 and Cj1298} and {Cj1120c, Cj1121c and Cj1123c}.

METHODS: All enzymes were overexpressed and purified before monitoring their activity by capillary electrophoresis. The cj1121c and cj1294 genes were disrupted by a chloramphenicol resistance …