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Tv-RIO1 – an atypical protein kinase from the parasitic nematode Trichostrongylus vitrinus

Hu, Min and LaRonde-LeBlanc, Nicole and Sternberg, Paul W. and Gasser, Robin B. (2008) Tv-RIO1 – an atypical protein kinase from the parasitic nematode Trichostrongylus vitrinus. Parasites and Vectors, 1 . Art. No. 34. ISSN 1756-3305. PMCID PMC2564912. https://resolver.caltech.edu/CaltechAUTHORS:HUMpv08

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Abstract

Background: Protein kinases are key enzymes that regulate a wide range of cellular processes, including cell-cycle progression, transcription, DNA replication and metabolic functions. These enzymes catalyse the transfer of phosphates to serine, threonine and tyrosine residues, thus playing functional roles in reversible protein phosphorylation. There are two main groups, namely eukaryotic protein kinases (ePKs) and atypical protein kinases (aPKs); RIO kinases belong to the latter group. While there is some information about RIO kinases and their roles in animals, nothing is known about them in parasites. This is the first study to characterise a RIO1 kinase from any parasite. Results: A full-length cDNA (Tv-rio-1) encoding a RIO1 protein kinase (Tv-RIO1) was isolated from the economically important parasitic nematode Trichostrongylus vitrinus (Order Strongylida). The uninterrupted open reading frame (ORF) of 1476 nucleotides encoded a protein of 491 amino acids, containing the characteristic RIO1 motif LVHADLSEYNTL. Tv-rio-1 was transcribed at the highest level in the third-stage larva (L3), and a higher level in adult females than in males. Comparison with homologues from other organisms showed that protein Tv-RIO1 had significant homology to related proteins from a range of metazoans and plants. Amino acid sequence identity was most pronounced in the ATP-binding motif, active site and metal binding loop. Phylogenetic analyses of selected amino acid sequence data revealed Tv-RIO1 to be most closely related to the proteins in the species of Caenorhabditis. A structural model of Tv-RIO1 was constructed and compared with the published crystal structure of RIO1 of Archaeoglobus fulgidus (Af-Rio1). Conclusion: This study provides the first insights into the RIO1 protein kinases of nematodes, and a foundation for further investigations into the biochemical and functional roles of this molecule in biological processes in parasitic nematodes.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1186/1756-3305-1-34DOIArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2564912/PubMed CentralArticle
ORCID:
AuthorORCID
Sternberg, Paul W.0000-0002-7699-0173
Additional Information:© 2008 Hu et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Received: 31 July 2008. Accepted: 22 September 2008. Published: 22 September 2008. This work was supported by the Australian Research Council (LP0667795 and LX0882231), Genetic Technologies Limited, Meat and Livestock Australia, the Australian Academy of Science, the Australian-American Fulbright Commission (RBG), and the Howard Hughes Medical Institute (PWS). Authors' contributions: RBG and MH conceived the project, collected the parasite material, analysed the data and drafted the manuscript. MH carried out the molecular work. NLL and PWS assisted in analyses, interpretation and the drafting of the manuscript. All authors read and approved the final manuscript. The authors declare that they have no competing interests.
Funders:
Funding AgencyGrant Number
Australian Research CouncilLP0667795
Australian Research CouncilLX0882231
Genetic Technologies LimitedUNSPECIFIED
Meat and Livestock AustraliaUNSPECIFIED
Australian Academy of ScienceUNSPECIFIED
Australian-American Fulbright CommissionUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
PubMed Central ID:PMC2564912
Record Number:CaltechAUTHORS:HUMpv08
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:HUMpv08
Usage Policy:This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
ID Code:11941
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:11 Oct 2008 07:15
Last Modified:03 Oct 2019 00:24

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