Functional Proteomics of Nuclear Proteins in Tetrahymena thermophila: A Review

Genes (Basel). 2019 May 1;10(5):333. doi: 10.3390/genes10050333.

Abstract

Identification and characterization of protein complexes and interactomes has been essential to the understanding of fundamental nuclear processes including transcription, replication, recombination, and maintenance of genome stability. Despite significant progress in elucidation of nuclear proteomes and interactomes of organisms such as yeast and mammalian systems, progress in other models has lagged. Protists, including the alveolate ciliate protozoa with Tetrahymena thermophila as one of the most studied members of this group, have a unique nuclear biology, and nuclear dimorphism, with structurally and functionally distinct nuclei in a common cytoplasm. These features have been important in providing important insights about numerous fundamental nuclear processes. Here, we review the proteomic approaches that were historically used as well as those currently employed to take advantage of the unique biology of the ciliates, focusing on Tetrahymena, to address important questions and better understand nuclear processes including chromatin biology of eukaryotes.

Keywords: affinity purification; chromatin biology; ciliates; mass spectrometry; nuclear processes; proteomics; protists.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cell Nucleus / genetics
  • Cell Nucleus / parasitology
  • Chromatin / genetics
  • Chromatin / parasitology
  • Ciliophora Infections / genetics*
  • Ciliophora Infections / parasitology
  • Cytoplasm / genetics
  • Cytoplasm / parasitology
  • Humans
  • Nuclear Proteins / genetics*
  • Proteomics*
  • Tetrahymena thermophila / genetics*
  • Tetrahymena thermophila / pathogenicity

Substances

  • Chromatin
  • Nuclear Proteins

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