期刊
CELLS
卷 11, 期 16, 页码 -出版社
MDPI
DOI: 10.3390/cells11162509
关键词
queuine; queuosine; tRNA modifications; Entamoeba histolytica; oxidative stress resistance
类别
资金
- Israel Science Foundation [3208/19]
- Ministry of Science and Technology, Israel [1020546]
- Niedersachsen-Deutsche Technion [ZN 3454]
- Singapore-MIT Alliance for Research and Technology, Antimicrobial Resistance IRG
- US National Institutes of Health [ES026856]
- Chulabhorn Graduate Institute
- Royal Golden Jubilee Ph.D. scholarship through the National Research Council of Thailand (NRCT) [PHD/0196/2561]
- JRS-TRF
Queuosine is a modified nucleoside that occurs in transfer RNA and eukaryotes must obtain it from their diet or gut microbiota. This study demonstrates that Entamoeba histolytica can salvage queuosine from certain bacteria and identifies the enzyme EhDUF2419 as crucial for this process. The findings also suggest that queuosine plays a role in protecting E. histolytica against oxidative stress.
Queuosine (Q) is a naturally occurring modified nucleoside that occurs in the first position of transfer RNA anticodons such as Asp, Asn, His, and Tyr. As eukaryotes lack pathways to synthesize queuine, the Q nucleobase, they must obtain it from their diet or gut microbiota. Previously, we described the effects of queuine on the physiology of the eukaryotic parasite Entamoeba histolytica and characterized the enzyme EhTGT responsible for queuine incorporation into tRNA. At present, it is unknown how E. histolytica salvages queuine from gut bacteria. We used liquid chromatography-mass spectrometry (LC-MS) and N-acryloyl-3-aminophenylboronic acid (APB) PAGE analysis to demonstrate that E. histolytica trophozoites can salvage queuine from Q or E. coli K12 but not from the modified E. coli QueC strain, which cannot produce queuine. We then examined the role of EhDUF2419, a protein with homology to DNA glycosylase, as a queuine salvage enzyme in E. histolytica. We found that glutathione S-transferase (GST)-EhDUF2419 catalyzed the conversion of Q into queuine. Trophozoites silenced for EhDUF2419 expression are impaired in their ability to form Q-tRNA from Q or from E. coli. We also observed that Q or E. coli K12 partially protects control trophozoites from oxidative stress (OS), but not siEhDUF2419 trophozoites. Overall, our data reveal that EhDUF2419 is central for the direct salvaging of queuine from bacteria and for the resistance of the parasite to OS.
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