| Title |
YcfDRM is a thermophilic oxygen-dependent ribosomal protein uL16 oxygenase
|
|---|---|
| Published in |
Extremophiles, March 2018
|
| DOI | 10.1007/s00792-018-1016-9 |
| Pubmed ID | |
| Authors |
Rok Sekirnik, Sarah E. Wilkins, Jacob Bush, Hanna Tarhonskaya, Martin Münzel, Aayan Hussein, Emily Flashman, Shabaz Mohammed, Michael A. McDonough, Christoph Loenarz, Christopher J. Schofield |
| Abstract |
YcfD from Escherichia coli is a homologue of the human ribosomal oxygenases NO66 and MINA53, which catalyse histidyl-hydroxylation of the 60S subunit and affect cellular proliferation (Ge et al., Nat Chem Biol 12:960-962, 2012). Bioinformatic analysis identified a potential homologue of ycfD in the thermophilic bacterium Rhodothermus marinus (ycfDRM). We describe studies on the characterization of ycfDRM, which is a functional 2OG oxygenase catalysing (2S,3R)-hydroxylation of the ribosomal protein uL16 at R82, and which is active at significantly higher temperatures than previously reported for any other 2OG oxygenase. Recombinant ycfDRM manifests high thermostability (Tm 84 °C) and activity at higher temperatures (Topt 55 °C) than ycfDEC (Tm 50.6 °C, Topt 40 °C). Mass spectrometric studies on purified R. marinus ribosomal proteins demonstrate a temperature-dependent variation in uL16 hydroxylation. Kinetic studies of oxygen dependence suggest that dioxygen availability can be a limiting factor for ycfDRM catalysis at high temperatures, consistent with incomplete uL16 hydroxylation observed in R. marinus cells. Overall, the results that extend the known range of ribosomal hydroxylation, reveal the potential for ycfD-catalysed hydroxylation to be regulated by temperature/dioxygen availability, and that thermophilic 2OG oxygenases are of interest from a biocatalytic perspective. |
X Demographics
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Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United Kingdom | 2 | 50% |
| Unknown | 2 | 50% |
Demographic breakdown
| Type | Count | As % |
|---|---|---|
| Scientists | 2 | 50% |
| Members of the public | 2 | 50% |
Mendeley readers
The data shown below were compiled from readership statistics for 18 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 18 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 6 | 33% |
| Student > Doctoral Student | 2 | 11% |
| Researcher | 2 | 11% |
| Student > Bachelor | 1 | 6% |
| Professor | 1 | 6% |
| Other | 3 | 17% |
| Unknown | 3 | 17% |
| Readers by discipline | Count | As % |
|---|---|---|
| Chemistry | 6 | 33% |
| Biochemistry, Genetics and Molecular Biology | 5 | 28% |
| Agricultural and Biological Sciences | 2 | 11% |
| Chemical Engineering | 2 | 11% |
| Unknown | 3 | 17% |
Attention Score in Context
This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 20 March 2018.
All research outputs
#13,507,266
of 23,026,672 outputs
Outputs from Extremophiles
#478
of 801 outputs
Outputs of similar age
#170,984
of 332,340 outputs
Outputs of similar age from Extremophiles
#8
of 16 outputs
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