Selective conservation of the RSL-encoding, proteinase inhibitory-type, clade L serpins in Caenorhabditis species.

Serpins are a highly conserved superfamily of serine and papain-like cysteine proteinase inhibitors that are divided phylogenetically into clades. Serpins also can be divided anatomically into those that reside predominately outside or inside cells. While the activities of the extracellular serpins are well understood, the biological functions, as well as the overall distribution of the intracellular (serpinIC) serpins is less well defined. Conceivably, the biological function of the serpinsIC might be revealed by analysis of species with genomes of lower complexity. To this end, we sought to define the clade L serpin repertoire of Caenorhabditis elegans and other nematode species. Analysis of the C. elegans genome revealed the presence of 9 serpin genes. Five genes encoded for full-length serpins with functional reactive site loops (RSL). By definition, these genes were designated proteinase inhibitory-type, RSL-encoding serpins. Four of the C. elegans genes encoded for proteins without an RSL or transcripts with premature termination codons. The high percentage of non-RSL encoding to RSL-encoding serpin genes suggested that the former served a unique biological function rather than residing in the genome as simple pseudogenes. If this hypothesis was correct, we expected these non-RSL encoding genes to be conserved precisely in other Caenorhabditis species. However, in contrast to the RSL-encoding serpins that were well conserved and segregated into 3 sub-clades, we failed to detect non-RSL encoding serpin orthologues in the genomes of Caenorhabditis briggsae and Caenorhabditis remanei. These data suggested that unlike their RSL-encoding paralogues, the relatively high percentage of non-RSL encoding serpins in C. elegans was a vestige of recent duplication events and these latter genes were unlikely to serve essential functions in Caenorhabditis species.