Volume 92, Issue 1, Pages 1-4 (January 1998)

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Volume 92, Issue 1, Pages 1-4 (January 1998) Protein Splicing of Inteins and Hedgehog Autoproteolysis: Structure, Function, and Evolution Francine B Perler Cell Volume 92, Issue 1, Pages 1-4 (January 1998) DOI: 10.1016/S0092-8674(00)80892-2

Figure 1 Intein Regions and Conserved Motifs An intein with a LAGLIDADG homing endonuclease is depicted with conserved motifs listed above and conserved residues involved in catalysis shown below. Nucleophiles are boxed. The splicing regions (open boxes) are separated by a linker or an endonuclease. Some inteins have a DNA recognition region (DRR, checkered box) present within the N-terminal splicing region. (Correction: N4 should be to the right of DRR.) Cell 1998 92, 1-4DOI: (10.1016/S0092-8674(00)80892-2)

Figure 2 The Mechanism of Protein Splicing The protein splicing pathway consists of four nucleophilic displacements. Molecules involved in protonation and deprotonation have been omitted. X represents the S or O atom of the Cys/Ser/Thr side chain. See text for details. Cell 1998 92, 1-4DOI: (10.1016/S0092-8674(00)80892-2)

Figure 3 The Hint Module The sequences of Drosophila Hh-C17, the Mxe GyrA mini-intein, and the Sce VMA intein were aligned based on structural similarities. The position of β strands are indicated by arrows and residues whose Cα atoms superimpose with Hh-C17 are in red. DRR and core endonuclease/linker regions are indicated with the number of residues in parenthesis. The three nucleophiles are in yellow boxes and the residues shown to facilitate the nucleophilic displacements are in blue boxes. Periods indicate spaces added to maximize structural alignment. To aid in comparison, all elements were numbered beginning with 1. Hh-C17 residues were renumbered as follows: C258 = C1, T326 = 69, H329 = 72, and D303 = 46. T199 (T + 1) and C455 (C + 1) are C-extein residues. The N2 intein motif does not align well with the structural elements and is not shown. Cell 1998 92, 1-4DOI: (10.1016/S0092-8674(00)80892-2)

Figure 4 A Scenario for Evolution of Inteins and Hh-C A primordial subdomain was duplicated and loop exchange occurred between subdomains to generate the Hint module. Inteins then acquired the DNA recognition region (DRR) and core endonuclease domain (ENDO) and Hh-C17 acquired a sterol recognition region (SRR). The order of these events is speculative. Adapted with permission from Hall et al., 1997. Cell 1998 92, 1-4DOI: (10.1016/S0092-8674(00)80892-2)