التفاصيل البيبلوغرافية
| العنوان: |
The first apicoplast tRNA thiouridylase plays a vital role in the growth of Toxoplasma gondii. |
| المؤلفون: |
Yimin Yang, Mi Lin, Xueqiu Chen, XianFeng Zhao, Lulu Chen, Mingxiu Zhao, Chaoqun Yao, Kaiyin Sheng, Yi Yang, Guangxu Ma, Aifang Du |
| المصدر: |
Frontiers in Cellular & Infection Microbiology; 8/15/2022, Vol. 12, p1-14, 14p |
| مصطلحات موضوعية: |
TRANSFER RNA, TOXOPLASMA gondii, LYTIC cycle, PARASITIC diseases, WARM-blooded animals, DRUG target |
| مستخلص: |
Toxoplasmosis caused by the protozoan Toxoplasma gondii is one of the most common parasitic diseases in humans and almost all warm-blooded animals. Lys, Glu, and Gln-specific tRNAs contain a super-modified 2-thiourea (s²U) derivatives at the position 34, which is essential for all living organisms by maintaining the structural stability and aminoacylation of tRNA, and the precision and efficiency of codon recognition during protein translation. However, the enzyme(s) involved in this modification in T. gondii remains elusive. In this report, three putative tRNA-specific 2- thiolation enzymes were identified, of which two were involved in the s²U34 modification of tRNALys, tRNAGlu, and tRNAGln. One was named TgMnmA, an apicoplast-located tRNA-specific 2-thiolation enzyme in T. gondii. Knockout of TgMnmA showed that this enzyme is important for the lytic cycle of tachyzoites. Loss of TgMnmA also led to abnormities in apicoplast biogenesis and severely disturbed apicoplast genomic transcription. Notably, mice survived from the infection with 10 TgMnmAKO RH tachyzoites. These findings provide new insights into s²U34 tRNA modification in Apicomplexa, and suggest TgMnmA, the first apicoplast tRNA thiouridylase identified in all apicomplexans, as a potential drug target. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
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