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Requirement for NusG for Transcription Antitermination In Vivo by the  N Protein.Ying Zhou, 2002.Transcription antitermination by the bacteriophage N protein is stimulated in vitro by the Escherichia coli NusG protein . Earlier work suggested that NusG was not required for N activity in vivo . Here we present evidence that NusG also stimulates N-mediated transcription antitermination in intact cells .
Flagellin Glycosylation Island in Pseudomonas syringae pv . glycinea and Its Role in Host Specificity. Kasumi Takeuchi, 2003.The deduced amino acid sequences of the flagellins of Pseudomonas syringae pv . tabaci and P . syringae pv . glycinea are identical; however, their abilities to induce a hypersensitive reaction are clearly different . The reason for the difference seems to depend on the posttranslational modification of the flagellins . To investigate the role of this posttranslational modification in the interactions between plants and bacterial pathogens, we isolated genes that are potentially involved in the posttranslational modification of flagellin in P . syringae pv . glycinea (glycosylation island); then defective mutants with mutations in these genes were generated . There are three open reading frames in the glycosylation island, designated orf1, orf2, and orf3 . orf1 and orf2 encode putative glycosyltransferases, and mutants with defects in these open reading frames,  orf1 and
orf2, secreted nonglycosylated and slightly glycosylated flagellins, respectively . Inoculation tests performed with these mutants and original nonhost tobacco leaves revealed that
orf1 and
orf2 could grow on tobacco leaves and caused symptom-like changes . In contrast, these mutants failed to cause symptoms on original host soybean leaves . These data indicate that putative glycosyltransferases encoded in the flagellin glycosylation island are strongly involved in recognition by plants and could be the specific determinants of compatibility between phytopathogenic bacteria and plant species .
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