Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.

Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase Gene Sequencing in Taxonomic Delineation of Padina Species in theNorthern Coast of the Persian Gulf, (IRAN)

Taxonomic study of the genus Padina (Dictyotales, Phaeophyceae) from the Persian Gulf coast was conducted based on morphology and molecular phylogenetic analyses using chloroplast encoded large subunit RuBisCo (rbcL) gene sequences. Detailed descriptions of each species found in this study are described. Several morphological characters, such as number of cell layers composing the thallus, pr...

Isolated Spinach Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Large Subunit εN- Methyltransferase and Method of Inactivating Ribulose-1,5-Bisphosphatase Carboxylase/ Oxygenase Large Subunit εN-Methyltransferase Activity

Plastome engineering of ribulose-1,5-bisphosphate carboxylase/oxygenase in tobacco to form a sunflower large subunit and tobacco small subunit hybrid.

Targeted gene replacement in plastids was used to explore whether the rbcL gene that codes for the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase, the key enzyme of photosynthetic CO2 fixation, might be replaced with altered forms of the gene. Tobacco (Nicotiana tabacum) plants were transformed with plastid DNA that contained the rbcL gene from either sunflower (Helianthus an...

Effects of a-amanitin on coordination of two mRNAs of ribulose-bisphosphate carboxylase in greening pea leaves

The effects of cr-amanitin on light induction of the two mRNAs of ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) in greening pea leaves were examined. Induction of the nuclear-coded small-subunit mRNA but not of the chloroplast-coded large-subunit mRNA was significantly reduced by a-amanitin, indicating that the steady-state level of the large-subunit mRNA is not directly affected by tha...

Preliminary structural studies of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) from Rhodospirillum rubrum has been crystallized in a form that is suitable for structural studies by x-ray diffraction. The asymmetric unit of the crystal contains one dimeric enzyme molecule of molecular mass 101,000 Da. The enzyme was activated prior to crystallization and is presumed to be in the CO2-activated state in the crysta...