A novel bacteriophage, PA-1, was isolated using Pantoea ananatis, a bacterium that is responsible for rice leaf blight worldwide, as the host. PA-1 has a linear genome of 46,332 bp with a GC content of 50.55%.
View Article and Find Full Text PDFBackground: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the chloroplast enzyme that fixes CO in photosynthesis, but the enzyme also fixes O, which leads to the wasteful photorespiratory pathway. If we better understand the structure-function relationship of the enzyme, we might be able to engineer improvements. When the crystal structure of Chlamydomonas Rubisco was solved, four new posttranslational modifications were observed which are not present in other species.
View Article and Find Full Text PDFGenes Genet Syst
November 2016
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a rate-limiting photosynthetic enzyme that catalyzes carbon fixation in the Calvin cycle. Much interest has been devoted to engineering this ubiquitous enzyme with the goal of increasing plant growth. However, experiments that have successfully produced improved Rubisco variants, via directed evolution in Escherichia coli, are limited to bacterial Rubisco because the eukaryotic holoenzyme cannot be produced in E.
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