Figure 2.

A full-length clone of a novel dynamin-like protein (DLP1) shares homology with dynamin and other dynamin-related proteins. (A) Amino acid sequence comparison of rat DLP1 with rat dynamin I, yeast Dnm1p, and Vps1p was performed by the Clustal method using the DNASTAR sequence analysis program. Conserved amino acid residues are boxed in black. The three regions with asterisks are GTP-binding elements. There is a high degree of homology within the NH₂-terminal domains, especially in the tripartite GTP-binding motif (asterisks), but all four sequences are completely divergent at the region aligned with the PH domain of dynamin I (aa 510–633 of Dyn1). Homology is partially restored at the extreme COOH-terminal end of DLP1. Proline-rich tails are not present in DLP1, Dnm1p, or Vps1p. (B) Table showing percent homology among dynamin-related proteins. Rat DLP1 shares up to 42% homology with other dynamin-related proteins. (C) Phylogenetic tree of the large GTPase superfamily showing that DLP1 is subgrouped with the yeast dynamin-related proteins.