Bacterial SET domain proteins and their role in eukaryotic chromatin modification

Álvarez-Venegas, Raúl

doi:10.3389/fgene.2014.00065

Cited by 41 publications

(37 citation statements)

References 42 publications

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“…S4) was upregulated. This may suggest that the predicted 16.46-kDa SET domain protein, a potential T3SS-secreted effector, might be “early” induced, to serve as a potential modulator of fungal gene expression [45]. Notably, transcription of a gene for a putative oxidoreductase, AKAUv1_530022, was upregulated (log2 fold change 1.93), next to that of a gene for a putative cytochrome c552 (log2 fold change 2.83; AKAUv1_2920083) (Fig.…”

Section: Resultsmentioning

confidence: 99%

Transcriptional Responses of the Bacterium Burkholderia terrae BS001 to the Fungal Host Lyophyllum sp. Strain Karsten under Soil-Mimicking Conditions

2016

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In this study, the mycosphere isolate Burkholderia terrae BS001 was confronted with the soil fungus Lyophyllum sp. strain Karsten on soil extract agar plates in order to examine its transcriptional responses over time. At the initial stages of the experiment (T1—day 3; T2—day 5), contact between both partner organisms was absent, whereas in the final stage (T3—day 8), the two populations made intimate physical contact. Overall, a strong modulation of the strain BS001 gene expression patterns was found. First, the stationary-phase sigma factor RpoS, and numerous genes under its control, were strongly expressed as a response to the soil extract agar, and this extended over the whole temporal regime. In the system, B. terrae BS001 apparently perceived the presence of the fungal hyphae already at the early experimental stages (T1, T2), by strongly upregulating a suite of chemotaxis and flagellar motility genes. With respect to specific metabolism and energy generation, a picture of differential involvement in different metabolic routes was obtained. Initial (T1, T2) up- or downregulation of ethanolamine and mandelate uptake and utilization pathways was substituted by a strong investment, in the presence of the fungus, in the expression of putative metabolic gene clusters (T3). Specifically at T3, five clustered genes that are potentially involved in energy generation coupled to an oxidative stress response, and two genes encoding short-chain dehydrogenases/oxidoreductases (SDR), were highly upregulated. In contrast, the dnaE2 gene (related to general stress response; encoding error-prone DNA polymerase) was transcriptionally downregulated at this stage. This study revealed that B. terrae BS001, from a stress-induced state, resulting from the soil extract agar milieu, responds positively to fungal hyphae that encroach upon it, in a temporally dynamic manner. The response is characterized by phases in which the modulation of (1) chemotaxis, (2) metabolic activity, and (3) oxidative stress responses are key mechanisms.Electronic supplementary materialThe online version of this article (doi:10.1007/s00248-016-0885-7) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Transcriptional Responses of the Bacterium Burkholderia terrae BS001 to the Fungal Host Lyophyllum sp. Strain Karsten under Soil-Mimicking Conditions

2016

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“…For example, the SET domain KMTs, which constitute close to a third of the MTases in humans (6), are rare in bacteria where they do not target endogenous bacterial proteins but rather act as effectors that modify histone proteins in the infected host (41). Accordingly, almost all the bacterial KMTs acting on endogenous proteins belong to the 7BS MTase family.…”

Section: Discussionmentioning

confidence: 99%

The METTL20 Homologue from Agrobacterium tumefaciens Is a Dual Specificity Protein-lysine Methyltransferase That Targets Ribosomal Protein L7/L12 and the β Subunit of Electron Transfer Flavoprotein (ETFβ)

Małecki

Dahl

Moen

et al. 2016

Journal of Biological Chemistry

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Human METTL20 is a mitochondrial, lysine-specific methyltransferase that methylates the ␤-subunit of electron transfer flavoprotein (ETF␤). Interestingly, putative METTL20 orthologues are found in a subset of ␣-proteobacteria, including Agrobacterium tumefaciens. Using an activity-based approach, we identified in bacterial extracts two substrates of recombinant METTL20 from A. tumefaciens (AtMETTL20), namely ETF␤ and the ribosomal protein RpL7/L12. We show that AtMETTL20, analogous to the human enzyme, methylates ETF␤ on Lys-193 and Lys-196 both in vitro and in vivo. ETF plays a key role in mediating electron transfer from various dehydrogenases, and we found that its electron transferring ability was diminished by AtMETTL20-mediated methylation of ETF␤. Somewhat surprisingly, AtMETTL20 also catalyzed monomethylation of RpL7/L12 on Lys-86, a common modification also found in many bacteria that lack METTL20. Thus, we here identify AtMETTL20 as the first enzyme catalyzing RpL7/ L12 methylation. In summary, here we have identified and characterized a novel bacterial lysine-specific methyltransferase with unprecedented dual substrate specificity within the seven ␤-strand class of lysine-specific methyltransferases, as it targets two apparently unrelated substrates, ETF␤ and RpL7/L12. Moreover, the present work establishes METTL20-mediated methylation of ETF␤ as the first lysine methylation event occurring in both bacteria and humans.

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“…The signalling pathways that activate the quintessential transcription factor NF-κB are so central to the inflammatory response, as well as cell proliferation and survival, that they seemed obvious candidates for parasite manipulation (Sun and Andersson, 2002). Indeed, parasites Heussler et al, 2002;Schmuckli-Maurer et al, 2010;Rosowski et al, 2011;Du et al, 2014p53 Bougdour et al, 20132014 Marsolier et al, 2013 appear to have developed several strategies to target different parts of the NF-κB pathways leading to interference with the transcription of many immune response genes. One example is the secretion of parasite effector proteins that directly initiate NF-κB signalling during To.…”

Section: Activating the Nuclear Factor-κb (Nf-κb) Pathwaymentioning

confidence: 99%

Host–parasite interactions: an intimate epigenetic relationship

Cheeseman

Weitzman

2015

Cell Microbiol

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SummaryThe epigenetics of host-pathogen interactions is emerging as an interesting angle from which to study how parasites have evolved sophisticated strategies to manipulate host gene transcription and protein expression. In this review, we discuss the application of an operational framework to investigate the host cell signalling pathways that are induced by intracellular parasites and the epigenomic consequences in the host nucleus. To illustrate this conceptual approach, we have focused on examples from two eukaryotic intracellular parasites of the apicomplexa phylum: Theileria and Toxoplasma. We review recent findings on intracellular parasitism strategies for hijacking host nuclear functions and discuss how we might think of the parasite and its proteome as an intracellular epigenator.

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Bacterial SET domain proteins and their role in eukaryotic chromatin modification

Cited by 41 publications

References 42 publications

Transcriptional Responses of the Bacterium Burkholderia terrae BS001 to the Fungal Host Lyophyllum sp. Strain Karsten under Soil-Mimicking Conditions

Transcriptional Responses of the Bacterium Burkholderia terrae BS001 to the Fungal Host Lyophyllum sp. Strain Karsten under Soil-Mimicking Conditions

The METTL20 Homologue from Agrobacterium tumefaciens Is a Dual Specificity Protein-lysine Methyltransferase That Targets Ribosomal Protein L7/L12 and the β Subunit of Electron Transfer Flavoprotein (ETFβ)

Host–parasite interactions: an intimate epigenetic relationship

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