Visualization of DNA-protein intermediates during activation of the Pu promoter of the TOL plasmid of Pseudomonas putida

Article Abstract:

DNA-protein intermediates in activation of the Pu promoter of the TOL plasmid of Pseudomonas putida has been visualized. Transmission electron microscopy was used to look at the ATP-dependent multimerization process undergone by the sigma(super.54) dependent activator XylR of the TOL plasmid pWW0 of P. putida when bound to the upstream activating sequences of the cognate Pu promoter. It appears, based on this study, that each time ATP is hydrolyzed the transcriptional activation complex is taken apart.

Usage, DNA, Plasmids, Bacterial genetics, Genetic regulation, Genetic transcription, Pseudomonas putida, Transcription (Genetics), Adenosine triphosphate, ATP, Variation (Biology), Transmission electron microscopes

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Cell cycle control of septin ring dynamics in the budding yeast

Article Abstract:

Cell cycle control of septin ring dynamics in budding yeast, Saccharomyces cerevisiae, is discussed. Septin-GFP fusion and time-lapse confocal microscopy were used to find that septin dynamics are maintained in budding zygotes and in unipolar synchronous growth in pseudohyphae. Septin assembly was found to be dependent on G1 cyclin/Cdc28-mediated cell cycle signals. The small GTPase Cdc42, but not Rho1, are essential for this. Findings support a role of cell cycle control mechanisms in the regulation of septin dynamics to accurately coordinate morphogenesis through the budding process in yeast.

Slovakia, Cell cycle, Yeast, Yeast (Food product)

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Structure of the ask-asd operon and formation of aspartokinase subunits in the cephamycin producer 'Amycolatopsis lactamdurans'

Article Abstract:

The ask-asd operon and its structure and formation of aspartokinase subunits have been studied in the cephamycin producer 'Amycolatopsis lactamdurans' The first two genes of the lysine pathway are linked closely to form a transcriptional operon in the organism. The asd gene encodes the enzyme aspartic semialdehyde dehydrogenase and encodes a 355 aa protein with deduced M 37109. The formation of two subunits of Ask from one gene, ask, has been confirmed using antibodies against the C-terminal end of Ask, identical in both subunits. Ask activity of the organism is regulated by the joint action of lysine and threonine. The inhibition is not seen in E. coli tranformants with Ser(super.301) to Tyr , or Gly to Asp mutation of hte A. lactamdurans ask gene.

Antibiotics, Enzymes, Bacteria, Streptomyces, Operons, Biosynthesis, Dehydrogenases, Oxidoreductases, Lysine

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