Phototaxis, chemotaxis and the missing link.
Phototaxis in Archaea employs an integral membrane complex composed of a photoreceptor that is similar to the light-driven proton pump bacteriorhodopsin, and a transducer protein that is similar to the familiar eubacterial chemotaxis receptors. Recent structural studies have revealed how these proteins are assembled in the membrane, and provide a heuristic framework for future work on the mechanism of signal transduction by this important class of molecules.
Oprian
Daniel D
DD
Department of Biochemistry and The Volen Center for Complex Systems, Brandeis University, Waltham, MA 02454, USA. oprian@brandeis.edu
D001105:Archaea / Q000502:physiology*; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002633:Chemotaxis; D008027:Light; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009068:Movement; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; C434451:HtrII protein, Natronobacterium pharaonis; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; C057635:Tsr protein, Bacteria