| RRC ID |
75576
|
| 著者 |
Ohira T, Minowa K, Sugiyama K, Yamashita S, Sakaguchi Y, Miyauchi K, Noguchi R, Kaneko A, Orita I, Fukui T, Tomita K, Suzuki T.
|
| タイトル |
Reversible RNA phosphorylation stabilizes tRNA for cellular thermotolerance.
|
| ジャーナル |
Nature
|
| Abstract |
Post-transcriptional modifications have critical roles in tRNA stability and function1-4. In thermophiles, tRNAs are heavily modified to maintain their thermal stability under extreme growth temperatures5,6. Here we identified 2'-phosphouridine (Up) at position 47 of tRNAs from thermophilic archaea. Up47 confers thermal stability and nuclease resistance to tRNAs. Atomic structures of native archaeal tRNA showed a unique metastable core structure stabilized by Up47. The 2'-phosphate of Up47 protrudes from the tRNA core and prevents backbone rotation during thermal denaturation. In addition, we identified the arkI gene, which encodes an archaeal RNA kinase responsible for Up47 formation. Structural studies showed that ArkI has a non-canonical kinase motif surrounded by a positively charged patch for tRNA binding. A knockout strain of arkI grew slowly at high temperatures and exhibited a synthetic growth defect when a second tRNA-modifying enzyme was depleted. We also identified an archaeal homologue of KptA as an eraser that efficiently dephosphorylates Up47 in vitro and in vivo. Taken together, our findings show that Up47 is a reversible RNA modification mediated by ArkI and KptA that fine-tunes the structural rigidity of tRNAs under extreme environmental conditions.
|
| 巻・号 |
605(7909)
|
| ページ |
372-379
|
| 公開日 |
2022-5-1
|
| DOI |
10.1038/s41586-022-04677-2
|
| PII |
10.1038/s41586-022-04677-2
|
| PMID |
35477761
|
| PMC |
PMC9095486
|
| MeSH |
Archaea* / genetics
Extreme Environments
Phosphorylation
RNA Processing, Post-Transcriptional
RNA, Archaeal / chemistry
RNA, Archaeal / metabolism
RNA, Transfer* / chemistry
RNA, Transfer* / metabolism
Thermotolerance*
Uridine
|
| リソース情報 |
| 一般微生物 |
JCM 8929
JCM 8930
JCM 9820
JCM 10595
JCM 19564 |
