The G protein gamma subunit. Requirements for dimerization with beta subunits.

The Journal of Biological Chemistry
U MendeE J Neer

Abstract

Guanine nucleotide-binding protein beta and gamma subunits form a tightly bound complex that can only be separated by denaturation. Assembly of beta and gamma subunits is a complicated process. The beta 1 and gamma 2 subunits can be synthesized in vitro in rabbit reticulocyte lysate and then assembled into dimers, but beta 1 cannot form beta gamma dimers when synthesized in a wheat germ extract. In contrast, gamma 2 translated in either system can dimerize with beta 1, suggesting that dimerization-competent gamma 2 can be synthesized without the aid of specific chaperonins or other cofactors. Dimerization-competent gamma 2 in solution forms an asymmetric particle with a Stokes radius of about 21 +/- 0.4 A (n = 4), s20,w of 0.9 S (range 0.8-1.0 S, n = 2), and frictional ratio of 1.57 (assuming no hydration). To define the part of gamma 2 that is needed for native beta gamma dimer formation, a series of N- and C-terminal truncations were generated, synthesized in vitro, and incubated with beta 1. Dimerization was assessed by stabilization of beta 1 to tryptic proteolysis. Truncation of up to 13 amino acids at the C terminus did not affect dimerization with beta 1, whereas removal of 27 amino acids prevented it. Therefore, a regio...Continue Reading

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