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. 2008 Feb 29;4(2):e1000022. doi: 10.1371/journal.pgen.1000022

Figure 1. Mutations in C. elegans eat-3 and dyn-1 Mutants.

Figure 1

(A) Dynamin family members in C. elegans. DYN-1 is required for scission of vesicles from the plasma membrane. DRP-1 is required for scission of mitochondrial outer membranes. FZO-1 is required for fusion of mitochondrial outer membranes. EAT-3 is required for fusion of mitochondrial inner membranes. The GTPase, Middle, and GTPase Effector (GED) domains are shared between dynamin family members. In addition, DYN-1 has a pleckstrin homology (PH) domain and a proline rich domain (PRD), FZO-1 has two transmembrane segments that anchor the protein in the mitochondrial outer membrane, and EAT-3 has a mitochondrial leader sequence (mls) that targets the protein to the mitochondrial intermembrane space. Some key alleles are shown on the right. (B) Sequence alignment of the GTPase domains of C. elegans EAT-3 (D2031.5), human Opa1, human Dyn1, and C. elegans DYN-1. The GTP binding consensus sequences (G1-4) are indicated with white circles. The primary mutations in eat-3(ad426) and dyn-1(ky51) alleles are shown in the red circles. Secondary mutations in the intragenic revertants are shown in the blue circles. The dyn-1(ky51) revertants cq2, cq3, and cq4 are shown below the sequences and the eat-3(ad426) revertants cq6, cq7, cq8, cq9, and cq10 are shown above the sequences. (C) The positions of the GTP binding motifs (open circles labeled G1-4), the positions of primary mutations (red circles), and the positions of secondary mutations (blue circles) superimposed on the structure of the rat Dyn1 GTPase domain [47]. The arrows point to the primary mutation suppressed by each secondary mutation.