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. 2006 Apr 21;2(4):e57. doi: 10.1371/journal.pgen.0020057

Figure 4. Protein Mutants Identified and Epistasis Tests.

Figure 4

(A) Alignment of a region of EGL-30 containing the M244I amino acid substitution with other G-proteins. The conserved methionine residue that is mutated to isoleucine in the egl-30(ep271) allele is indicated in bold text and underlined.

(B) Diagram showing the domain structure of the EAT-16 protein with relative locations of the E158K substitution found in the eat-16(ep273) allele, and the splice site mutation found in eat16(ad702) strains.

(C) Genetic interactions between mutations in G-αq and RGS. The G-αq/egl-30(ep271) and RGS/eat-16(ad702) mutations confer resistance to BMS-192364. The sensitivity of a G-αq/egl-30(pk931) strain to BMS-192364 is abrogated in the presence of the eat-16(ad702) mutation.