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Solution structure of a ubiquitin-like protein from Trypanosoma brucei.

ABSTRACT: Ubiquitin-like proteins, similar to ubiquitin, can either exist freely or be covalently attached to other proteins via an enzymatic cascade. The ubiquitin-like proteins play roles in multiple biological processes including transcription, stress responses, DNA repair and so on. In this study, a novel ubiquitin-like protein (TbUbl11) was identified in Trypanosoma brucei. The solution structure of TbUbl11 was solved by NMR spectroscopy. TbUbl11 adopts a conserved ?-grasp fold composed by a five-stranded ?-sheet curling around a central ?-helix, similar to other ubiquitin-like proteins. Meanwhile, some differences between TbUbl11 and other ubiquitin-like proteins were also identified. Additionally, we revealed that TbUbl11 is located in the whole cell body of procyclic-form T. brucei.

SUBMITTER: Mi J

PROVIDER: S-EPMC6199154 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Solution structure of a ubiquitin-like protein from Trypanosoma brucei.

Mi Juan J Zhang Jiahai J Liao Shanhui S Tu Xiaoming X

Protein science : a publication of the Protein Society 20181003 10

Ubiquitin-like proteins, similar to ubiquitin, can either exist freely or be covalently attached to other proteins via an enzymatic cascade. The ubiquitin-like proteins play roles in multiple biological processes including transcription, stress responses, DNA repair and so on. In this study, a novel ubiquitin-like protein (TbUbl11) was identified in Trypanosoma brucei. The solution structure of TbUbl11 was solved by NMR spectroscopy. TbUbl11 adopts a conserved β-grasp fold composed by a five-str ...[more]

PMID: 30058168

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Project description:UnlabelledTbRRM1 of Trypanosoma brucei is a nucleoprotein that was previously identified in a search for splicing factors in T. brucei. We show that TbRRM1 associates with mRNAs and with the auxiliary splicing factor polypyrimidine tract-binding protein 2, but not with components of the core spliceosome. TbRRM1 also interacts with several retrotransposon hot spot (RHS) proteins and histones. RNA immunoprecipitation of a tagged form of TbRRM1 from procyclic (insect) form trypanosomes identified ca. 1,500 transcripts that were enriched and 3,000 transcripts that were underrepresented compared to cellular mRNA. Enriched transcripts encoded RNA-binding proteins, including TbRRM1 itself, several RHS transcripts, mRNAs with long coding regions, and a high proportion of stage-regulated mRNAs that are more highly expressed in bloodstream forms. Transcripts encoding ribosomal proteins, other factors involved in translation, and procyclic-specific transcripts were underrepresented. Knockdown of TbRRM1 by RNA interference caused widespread changes in mRNA abundance, but these changes did not correlate with the binding of the protein to transcripts, and most splice sites were unchanged, negating a general role for TbRRM1 in splice site selection. When changes in mRNA abundance were mapped across the genome, regions with many downregulated mRNAs were identified. Two regions were analyzed by chromatin immunoprecipitation, both of which exhibited increases in nucleosome occupancy upon TbRRM1 depletion. In addition, subjecting cells to heat shock resulted in translocation of TbRRM1 to the cytoplasm and compaction of chromatin, consistent with a second role for TbRRM1 in modulating chromatin structure.ImportanceTrypanosoma brucei, the parasite that causes human sleeping sickness, is transmitted by tsetse flies. The parasite progresses through different life cycle stages in its two hosts, altering its pattern of gene expression in the process. In trypanosomes, protein-coding genes are organized as polycistronic units that are processed into monocistronic mRNAs. Since genes in the same unit can be regulated independently of each other, it is believed that gene regulation is essentially posttranscriptional. In this study, we investigated the role of a nuclear RNA-binding protein, TbRRM1, in the insect stage of the parasite. We found that TbRRM1 binds nuclear mRNAs and also affects chromatin status. Reduction of nuclear TbRRM1 by RNA interference or heat shock resulted in chromatin compaction. We propose that TbRRM1 regulates RNA polymerase II-driven gene expression both cotranscriptionally, by facilitating transcription and efficient splicing, and posttranscriptionally, via its interaction with nuclear mRNAs.

Dataset Information

Solution structure of a ubiquitin-like protein from Trypanosoma brucei.

Publications

Solution structure of a ubiquitin-like protein from Trypanosoma brucei.

Similar Datasets

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