Functional expression of pharaonis phoborhodopsin in Escherichia coli.
Pharaonis phoborhodopsin, the photoreceptor of the negative phototaxis of archaebacterial Natronobacterium pharaonis, was functionally expressed in the heterologous system of Escherichia coli. Flash-photolysis on a millisecond time scale indicated that the photochemical properties of ppR expressed in E. coli were the same as those of the native ppR in N. pharaonis. We concluded that the integral membrane protein ppR is correctly folded in vivo in the eubacterial E. coli membrane.
Shimono
K
K
Laboratory of Biophysical Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Iwamoto
M
M
Sumi
M
M
Kamo
N
N
D019843:Archaeal Proteins; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000235:genetics*; D002338:Carotenoids; D002462:Cell Membrane; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D019766:Genes, Archaeal / Q000235:genetics; D025602:Halorhodopsins; D019633:Natronobacterium / Q000235:genetics*; D010782:Photolysis; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D025603:Sensory Rhodopsins
D019843:Archaeal Proteins; D025602:Halorhodopsins; D011993:Recombinant Fusion Proteins; D025603:Sensory Rhodopsins; C061508:sensory rhodopsin II protein, archaeal; D002338:Carotenoids; D001436:Bacteriorhodopsins