Interaction of transducin with light-activated rhodopsin protects It from proteolytic digestion by trypsin.

The Journal of Biological Chemistry
M R Mazzoni, Heidi E Hamm

Abstract

The tryptic cleavage pattern of transducin (Gt) in solution was compared with that in the presence of phospholipid vesicles, rod outer segment (ROS) membranes kept in the dark, or ROS membranes containing light-activated rhodopsin, metarhodopsin II (Rh*). When Gt was in the high affinity complex with Rh*, the alphat subunit was almost completely protected from proteolysis. The protection of alphat at Arg310 was complete, while Arg204 was substantially protected. The cleavage of alphat at Lys18 was protected in the presence of phospholipid vesicles, ROS membranes kept in the dark, or ROS membranes containing Rh*. The cleavage of betat was slower in the presence of ROS membranes or phospholipid vesicles. When the Rh*. Gt complex was incubated with guanyl-5'-yl thiophosphate, a guanine nucleotide analog known to release the high affinity interaction between Gt and Rh*, the protection at Arg310 and Arg204 was diminished. From our results, we propose that Rh* either physically blocks access of trypsin to Arg204 and Arg310 or maintains the heterotrimer in such a conformation that these cleavage sites are not available. Since Arg204 is involved in the switch interface with betagammat (Lambright, D. G., Sondek, J., Bohm, A., Skiba, N. ...Continue Reading

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Feb 2, 2010·Journal of Molecular Modeling·Andrea Strasser, Hans-Joachim Wittmann
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