Hervás M, Navarro F, Navarro J A, Chávez S, Díaz A, Florencio F J, De la Rosa M A
Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla y CSIC, Spain.
FEBS Lett. 1993 Mar 22;319(3):257-60. doi: 10.1016/0014-5793(93)80558-c.
Native plastocyanin from Synechocystis 6803 has been isolated and purified to electrophoretic homogeneity. The corresponding gene (petE) has been cloned and expressed in E. coli, thus leading to a protein completely identical to plastocyanin purified from the cyanobacterial cells. The petE gene product is correctly processed in E. coli as deduced from the N-terminal amino acid sequences. These results, along with the identical physicochemical and kinetic properties of the two protein preparations, confirm that expression of petE in E. coli is an adequate tool to address the study of Synechocystis plastocyanin by site-directed mutagenesis.
