A type-1 metacaspase from Acanthamoeba castellanii |
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Authors: | Trzyna Wendy C Legras Xavier D Cordingley John S |
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Affiliation: | aDepartment of Biological Sciences, Louisiana Tech University, PO Box 3179, Ruston, Louisiana, LA 71 272, USA |
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Abstract: | The complete sequence of a type-1 metacaspase from Acanthamoeba castellanii is reported comprising 478 amino acids. The metacaspase was recovered from an expression library using sera specific for membrane components implicated in stimulating encystation. A central domain of 155 amino acid residues contains the Cys/His catalytic dyad and is the most conserved region containing at least 30 amino acid identities in all metacaspases. The Acanthamoeba castellanii metacaspase has the most proline-rich N-terminus so far reported in type-1 metacaspases with over 40 prolines in the first 150 residues. Ala–Pro–Pro is present 11 times. Phylogenies constructed using only the conserved proteolytic domains or the complete sequences show identical branching patterns, differing only in the rates of change. |
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Keywords: | Acanthamoeba castellanii Type-1 metacaspase Encystation Signaling complex |
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