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Molecular & Cellular Proteomics

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Global lysine crotonylation and 2-hydroxyisobutyrylation in phenotypically different Toxoplasma gondii parasites

Deqi Yin, Yue Zhang, Dawei Wang, Xiaoyu Sang, Ying Feng, Ran Chen, Xinyi Wang, Na Yang, Ning Jiang and View ORCID ProfileQijun Chen  Correspondence email
Molecular & Cellular Proteomics September 5, 2019, mcp.RA119.001611; https://doi.org/10.1074/mcp.RA119.001611
Deqi Yin
Shenyang Agricultural University, China
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Yue Zhang
Shenyang Agricultural University, China
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Dawei Wang
Shenyang Agricultural University, China
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Xiaoyu Sang
Shenyang Agricultural University, China
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Ying Feng
Shenyang Agricultural University, China
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Ran Chen
Shenyang Agricultural University, China
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Xinyi Wang
Shenyang Agricultural University, China
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Na Yang
Shenyang Agricultural University, China
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Ning Jiang
Shenyang Agricultural University, China
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Qijun Chen
Shenyang Agricultural University, China
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  • ORCID record for Qijun Chen
  • For correspondence: qijunchen759@syau.edu.cn
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Abstract

Toxoplasma gondii is a unicellular protozoan parasite of the phylum Apicomplexa. The parasite repeatedly goes through a cycle of invasion, division and induction of host cell rupture, which is an obligatory process for proliferation inside warm-blooded animals. It is known that the biology of the parasite is controlled by a variety of mechanisms ranging from genomic to epigenetic to transcriptional regulation. In this study, we investigated the global protein posttranslational lysine crotonylation and 2-hydroxyisobutyrylation of two T. gondii strains, RH and ME49, which represent distinct phenotypes for proliferation and pathogenicity in the host. Proteins with differential expression and modification patterns associated with parasite phenotypes were identified. Many proteins in T. gondii were crotonylated and 2-hydroxyisobutyrylated, and they were localized in diverse subcellular compartments involved in a wide variety of cellular functions such as motility, host invasion, metabolism and epigenetic gene regulation. These findings suggest that lysine crotonylation and 2-hydroxyisobutyrylation are ubiquitous throughout the T. gondii proteome, regulating critical functions of the modified proteins. These data provide a basis for identifying important proteins associated with parasite development and pathogenicity.

  • Toxoplasma gondii
  • proteome
  • posttranslational modification
  • phenotype
  • regulation
  • Parasite
  • Pathway Analysis
  • Protein-Protein Interactions*
  • Proteogenomics
  • Virulence

Footnotes

  • Author contributions: D.Y. and Q.C. analyzed data; Y.Z., D.W., X.S., Y.F., R.C., X.W., N.Y., and N.J. performed research; Q.C. designed research; Q.C. contributed new reagents/analytic tools; Q.C. wrote the paper.

  • Received June 6, 2019.
  • Revision received September 4, 2019.
  • Accepted September 5, 2019.
  • Published under license by The American Society for Biochemistry and Molecular Biology, Inc.
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Global lysine crotonylation and 2-hydroxyisobutyrylation in phenotypically different Toxoplasma gondii parasites
Deqi Yin, Yue Zhang, Dawei Wang, Xiaoyu Sang, Ying Feng, Ran Chen, Xinyi Wang, Na Yang, Ning Jiang, Qijun Chen
Molecular & Cellular Proteomics September 5, 2019, mcp.RA119.001611; DOI: 10.1074/mcp.RA119.001611

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Global lysine crotonylation and 2-hydroxyisobutyrylation in phenotypically different Toxoplasma gondii parasites
Deqi Yin, Yue Zhang, Dawei Wang, Xiaoyu Sang, Ying Feng, Ran Chen, Xinyi Wang, Na Yang, Ning Jiang, Qijun Chen
Molecular & Cellular Proteomics September 5, 2019, mcp.RA119.001611; DOI: 10.1074/mcp.RA119.001611
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