Synechocystis 6803 plastocyanin isolated from both the cyanobacterium and E. coli transformed cells are identical.
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.
Hervás
M
M
Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla y CSIC, Spain.
Navarro
F
F
Navarro
J A
JA
Chávez
S
S
Díaz
A
A
Florencio
F J
FJ
De la Rosa
M A
MA
D000595:Amino Acid Sequence; D001483:Base Sequence; D000458:Cyanobacteria / Q000737:chemistry*; D004926:Escherichia coli; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D010970:Plastocyanin / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013057:Spectrum Analysis
D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins; D010970:Plastocyanin