4.3 Article

Analyses of Compact Trichinella Kinomes Reveal a MOS-Like Protein Kinase with a Unique N-Terminal Domain

期刊

G3-GENES GENOMES GENETICS
卷 6, 期 9, 页码 2847-2856

出版社

GENETICS SOCIETY AMERICA
DOI: 10.1534/g3.116.032961

关键词

parasitic worms; Trichinella; kinome; protein kinases; protein annotation

资金

  1. National Health and Medical Research Council (NHMRC)
  2. Australian Research Council
  3. Wellcome Trust
  4. University of Melbourne Business Improvement Program
  5. Australian Academy of Science
  6. Australian-American Fulbright Commission
  7. Alexander von Humboldt Foundation
  8. Melbourne Water Corporation
  9. Victorian Life Sciences Computation Initiative
  10. WormBase
  11. Howard Hughes Medical Institute
  12. National Institutes of Health
  13. University of Melbourne
  14. NHMRC

向作者/读者索取更多资源

Parasitic worms of the genus Trichinella (phylum Nematoda; class Enoplea) represent a complex of at least twelve taxa that infect a range of different host animals, including humans, around the world. They are foodborne, intracellular nematodes, and their life cycles differ substantially from those of other nematodes. The recent characterization of the genomes and transcriptomes of all twelve recognized taxa of Trichinella now allows, for the first time, detailed studies of their molecular biology. In the present study, we defined, curated, and compared the protein kinase complements (kinomes) of Trichinella spiralis and T. pseudospiralis using an integrated bioinformatic workflow employing transcriptomic and genomic data sets. We examined how variation in the kinome might link to unique aspects of Trichinella morphology, biology, and evolution. Furthermore, we utilized in silico structural modeling to discover and characterize a novel, MOS-like kinase with an unusual, previously undescribed N-terminal domain. Taken together, the present findings provide a basis for comparative investigations of nematode kinomes, and might facilitate the identification of Enoplea-specific intervention and diagnostic targets. Importantly, the in silico modeling approach assessed here provides an exciting prospect of being able to identify and classify currently unknown (orphan) kinases, as a foundation for their subsequent structural and functional investigation.

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