論文 - 詳細
| RRC ID | 35546 |
|---|---|
| 著者 | Miyauchi K, Kimura S, Suzuki T. |
| タイトル | A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification. |
| ジャーナル | Nat Chem Biol |
| Abstract |
N(6)-threonylcarbamoyladenosine (t(6)A) is a universally conserved, essential modified nucleoside found in transfer RNAs (tRNAs) responsible for ANN codons in all three domains of life. t(6)A has a crucial role in maintaining decoding accuracy during protein synthesis. The presence of t(6)A in cellular tRNAs has been well documented for more than four decades. However, under conditions optimized for nucleoside preparation, we detected little t(6)A in tRNAs from Escherichia coli. Instead, we identified a new modified base named 'cyclic t(6)A' (ct(6)A), which is a cyclized active ester with an oxazolone ring. An E1-like enzyme, CsdL (renamed as TcdA), which catalyzes ATP-dependent dehydration of t(6)A to form ct(6)A, was also identified. Two yeast homologs of tcdA, YHR003C (TCD1) and YKL027W (TCD2), were required for ct(6)A formation and respiratory cell growth. ct(6)A was involved in promoting decoding efficiency. Structural modeling suggests that ct(6)A recognizes the first adenine base of ANN codon at the ribosomal A site. |
| 巻・号 | 9(2) |
| ページ | 105-11 |
| 公開日 | 2013-2-1 |
| DOI | 10.1038/nchembio.1137 |
| PII | nchembio.1137 |
| PMID | 23242255 |
| MeSH | Adenosine / analogs & derivatives* Adenosine / chemistry Adenosine Triphosphate / chemistry Catalysis Codon Escherichia coli / enzymology Escherichia coli Proteins / metabolism Hydrolysis Magnetic Resonance Spectroscopy Models, Chemical Models, Genetic Nucleic Acid Conformation Oxazolone / chemistry Protein Biosynthesis Protein Structure, Secondary RNA, Transfer / chemistry* Recombinant Proteins / chemistry Ubiquitin-Activating Enzymes / metabolism |
| IF | 12.587 |
| 引用数 | 94 |
| WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 11 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 原核生物(大腸菌) | NA |