Serpins in UnicellularEukarya,Archaea, andBacteria:Sequence Analysis and Evolution

Roberts, Thomas; Hejgaard, Jørn; Saunders, Neil; Cavicchioli, Ricardo; Curmi, Paul
October 2004
Journal of Molecular Evolution;Oct2004, Vol. 59 Issue 4, p437
Academic Journal
Most serpins irreversibly inactivate specific serine proteinases of the chymotrypsin family. Inhibitory serpins are unusual proteins in that their native structure is metastable, and rapid conversion to a relaxed state is required to trap target enzymes in a covalent complex. The evolutionary origin of the serpin fold is unresolved, and while serpins in animals are known to be involved in the regulation of a remarkable diversity of metabolic processes, the physiological functions of homologues from other phyla are unknown. Addressing these questions, here we analyze serpin genes identified in unicellular eukaryotes: the green algaChlamydomonas reinhardtii, the dinoflagellateAlexandrium tamarense, and the human pathogensEntamoebaspp.,Eimera tenella,Toxoplasma gondii, andGiardia lamblia. We compare these sequences to others, particularly those in the complete genome sequences ofArchaea, where serpins were found in only 4 of 13 genera, andBacteria, in only 9 of 56 genera. The serpins from unicellular organisms appear to be phylogenetically distinct from all of the clades of higher eukaryotic serpins. Most of the sequences from unicellular organisms have the characteristics of inhibitory serpins, and where multiple serpin genes are found in one genome, variability is displayed in the region of the reactive-center loop important for specificity. All the unicellular eukaryotic serpins have large hydrophobic or positively charged residues at the putative P1 position. In contrast, none of the prokaryotic serpins has a residue of these types at the predicted P1 position, but many have smaller, neutral residues. Serpin evolution is discussed.


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