Eukaryote-conserved histone post-translational modification landscape in Giardia duodenalis revealed by mass spectrometry

Emery-Corbin, Samantha J.; Hamey, Joshua J.; Balan, Balu; Rojas-López, Laura; Svärd, Staffan G.; Jex, Aaron R.

doi:10.1016/j.ijpara.2020.09.006

Cited by 10 publications

(11 citation statements)

References 115 publications

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“…As in other eukaryotes, the Giardia core histones contain intrinsically disordered “tail” regions that undergo conserved post-translational modifications. Emery-Corbin and colleagues identified Giardia histone modifications, including methylation, acetylation, and phosphorylation, using mass spectrometry [ 60 ]. They demonstrated that Giardia histone tails are highly modified (more than 50 sites were identified) and that these histone modifications in Giardia are largely equivalent to those in many other eukaryotes, suggesting that similar epigenetic mechanisms exist in this parasite [ 60 ].…”

Section: Structures Of Nucleosomes Containing Parasite Histonesmentioning

confidence: 99%

“…Emery-Corbin and colleagues identified Giardia histone modifications, including methylation, acetylation, and phosphorylation, using mass spectrometry [ 60 ]. They demonstrated that Giardia histone tails are highly modified (more than 50 sites were identified) and that these histone modifications in Giardia are largely equivalent to those in many other eukaryotes, suggesting that similar epigenetic mechanisms exist in this parasite [ 60 ]. Among the well-conserved modifications, the phosphorylation of H3 Ser10, and the methylations of H3 Lys4, Lys36, Lys9 and Lys27, but not H3 Lys79 and H4 Lys20, were identified in Giardia .…”

Section: Structures Of Nucleosomes Containing Parasite Histonesmentioning

confidence: 99%

“…The functions of the acidic patch and the H2B insertion in Giardia cells are unknown. A comprehensive analysis revealed the phosphorylations of H2B Ser45 in the six-residue insertion and the adjacent Thr49, which are unique residues in Giardia [ 60 ], although their functions remain unknown. In addition, some counterparts of acidic patch recognition proteins, including Dot1L, SET8, and RCC1, have not been identified [ 38 ].…”

Section: Structures Of Nucleosomes Containing Parasite Histonesmentioning

confidence: 99%

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Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses

2022

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In eukaryotes, genomic DNA is bound with histone proteins and packaged into chromatin. The nucleosome, a fundamental unit of chromatin, regulates the accessibility of DNA to enzymes involved in gene regulation. During the past few years, structural analyses of chromatin architectures have been limited to evolutionarily related organisms. The amino acid sequences of histone proteins are highly conserved from humans to yeasts, but are divergent in the deeply branching protozoan groups, including human parasites that are directly related to human health. Certain large DNA viruses, as well as archaeal organisms, contain distant homologs of eukaryotic histone proteins. The divergent sequences give rise to unique and distinct nucleosome architectures, although the fundamental principles of histone folding and DNA contact are highly conserved. In this article, we review the structures and biophysical properties of nucleosomes containing histones from the human parasites Giardia lamblia and Leishmania major, and histone-like proteins from the Marseilleviridae amoeba virus family. The presented data confirm the sharing of the overall DNA compaction system among evolutionally distant species and clarify the deviations from the species-specific nature of the nucleosome.

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Section: Structures Of Nucleosomes Containing Parasite Histonesmentioning

confidence: 99%

Section: Structures Of Nucleosomes Containing Parasite Histonesmentioning

confidence: 99%

Section: Structures Of Nucleosomes Containing Parasite Histonesmentioning

confidence: 99%

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Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses

2022

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“…In Giardia , epigenetic mechanisms are involved in the regulation of encystation, antigenic regulation, and resistance to antibiotics (Lagunas‐Rangel & Bermúdez‐Cruz, 2019). Furthermore, epigenetic marks in histones are associated with effects on gene expression in Giardia (Carranza et al., 2016; Emery‐Corbin et al., 2020; Lagunas‐Rangel et al., 2021). Histone acetylation, a well‐studied example of histone marks, is associated with active chromatin and gene transcription, whereas histone deacetylation is associated with inactive chromatin and repression of gene transcription.…”

Section: Introductionmentioning

confidence: 99%

Sirtuin GdSir2.4 participates in the regulation of rRNA transcription in the Giardia duodenalis parasite

Lagunas‐Rangel

Yee

García‐Villa

et al. 2021

Molecular Microbiology

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Giardia duodenalis is a parasite of great medical interest due to the number of infections it causes worldwide each year. Although research on epigenetic mechanisms in this protist has only begun recently, epigenetic regulation has already been shown to have important roles in encystation, antigenic variation, and resistance to antibiotics in Giardia. In this work, we show that a Giardia ortholog of Sir2, GdSir2.4, is involved in the silencing of rRNA expression. Our results demonstrate that GdSir2.4 localizes to the nucleolus, and its binding to the intergenic spacer region of the rDNA is associated with the deacetylation of the chromatin in this region. Given the importance of the regulation of rRNA expression to maintain adequate levels of ribosomes and genomic stability within the cells, GdSir2.4 can be considered a target to create new therapeutic agents against this parasite.

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“…This is of pharmacological importance given the association of human histone methylation enzymes with disease etiology ( 35 , 36 , 37 ) and their emergence as promising therapeutic targets for anticancer drug development ( 38 , 39 , 40 , 41 ). Histone methylation sites and enzymes are also conserved, albeit to varying extents, in lower eukaryotes that impact on human health, such as protozoans ( 42 , 43 , 44 ). Budding yeast also serves as an excellent model for epigenetic gene regulation in these species and may therefore provide insights into the design of antiparasitic drugs.…”

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confidence: 99%

Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast

Separovich

Wilkins

2021

Journal of Biological Chemistry

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

show abstract

Eukaryote-conserved histone post-translational modification landscape in Giardia duodenalis revealed by mass spectrometry

Cited by 10 publications

References 115 publications

Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses

Nucleosome Structures Built from Highly Divergent Histones: Parasites and Giant DNA Viruses

Sirtuin GdSir2.4 participates in the regulation of rRNA transcription in the Giardia duodenalis parasite

Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast

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