The atypical serine protein kinase RIOK-2, one of four members of the RIOK family (RIOK-1, RIOK-2, RIOK-3 and RIOK-B), named for the right open reading frame 1 domain in the prototype member of this family, RIOK-1 from yeast 1. stercoralis and of parasitic nematodes generally, and provides a foundation for further functional genomic studies. This study demonstrates significant advancement in molecular and cellular biological study of S.
Expression driven by this promoter predominated in intestinal cells. stercoralis, we observed expression patterns of a transgene construct encoding green fluorescent protein under the Ss-riok-2 promoter in post free-living S. To identify anatomical patterns of Ss-riok-2 expression in S. RNAseq analysis revealed the highest levels of the Ss-riok-2 transcript in free-living females and parasitic females. The putative promoter of Ss-riok-2 contains a number of conserved elements.
A docking study revealed some critical sites for ATP binding and metal binding. A three-dimensional structure (3D) model of Ss-RIOK-2 was generated using the Chaetomium thermophilum RIOK-2 protein kinase ( Ct-RIOK-2) crystal structure 4GYG as a template. In the present study, we have isolated and characterized the full-length cDNA, gDNA and a putative promoter of a RIOK-2 protein kinase ( Ss-RIOK-2) encoding gene ( Ss-riok-2) from Strongyloides stercoralis, a medically important parasitic nematode (Order Rhabditida). However, little is known about their functions in parasitic nematodes. RIO kinases are essential atypical protein kinases in diverse prokaryotic and eukaryotic organisms, playing significant roles in yeast and humans.
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