Isolation of a prokaryotic photoreceptor: sensory rhodopsin from halobacteria

AUTOR(ES)

Schegk, E. Sebastian

RESUMO

The photoreceptor sensory rhodopsin was isolated from halobacterial cell membranes solubilized in laurylmaltoside. In the presence of retinal, detergent and salt the native protein was obtained in pure form by sucrose density gradient centrifugation, hydroxyapatite chromatography and gel filtration. The apparent mol. wt of the molecule was 24 kd if analysed by SDS gel electrophoresis, and 49 kd by sedimentation and size-exclusion chromatographic analysis. The chromoprotein had an absorption maximum at 580 nm which was 8 nm blueshifted compared to the membrane-bound state. The molecule was photochemically active and the action spectrum for formation of SR380, the long-lived intermediate, coincided with the absorption spectrum.

Documentos Relacionados

• Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor.
• The photoreceptor sensory rhodopsin I as a two-photon-driven proton pump.
• Structure of a bacterial BLUF photoreceptor: Insights into blue light-mediated signal transduction
• Chlamyrhodopsin represents a new type of sensory photoreceptor.
• The methyl-accepting transducer protein HtrI is functionally associated with the photoreceptor sensory rhodopsin I in the archaeon Halobacterium salinarium.