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1 September 2001 Pharaonis Phoborhodopsin Binds to its Cognate Truncated Transducer Even in the Presence of a Detergent with a 1:1 Stoichiometry
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Abstract

Pharaonis phoborhodopsin (ppR) (also pharaonis sensory rhodopsin II) is a receptor of the negative phototaxis of Natronobacterium pharaonis. ppR forms a complex with its pharaonis halobacterial transducer (pHtrII), and this complex transmits the light signal to the sensory system in the cytoplasm. The expressed C-terminal-His tagged ppR and C-terminal-His tagged truncated pHtrII (t-Htr) in Escherichia coli (His means the 6× histidine tag) form a complex even in the presence of 0.1% of n-dodecyl-β-d-maltoside, and the M-decay of the complex became about twice slower than that of ppR alone. The photocycling rates under varying concentration ratios of ppR to t-Htr in the presence of detergent were measured. The data were analyzed on the following assumptions: (1) the M-decay of both ppR alone and the complex followed a single exponential decay with different time constants; and (2) the M-decay under varying concentration ratios of ppR to t-Htr, therefore, followed a biexponential decay function which combined the decay of the free ppR and that of the complex as photoreactive species. From these analyses we estimated the dissociation constant (15.2 ± 1.8 μM) and the number of binding sites (1.2 ± 0.08).

Yuki Sudo, Masayuki Iwamoto, Kazumi Shimono, and Naoki Kamo "Pharaonis Phoborhodopsin Binds to its Cognate Truncated Transducer Even in the Presence of a Detergent with a 1:1 Stoichiometry," Photochemistry and Photobiology 74(3), 489-494, (1 September 2001). https://doi.org/10.1562/0031-8655(2001)074<0489:PPBTIC>2.0.CO;2
Received: 8 March 2001; Accepted: 1 May 2001; Published: 1 September 2001
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