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TitleGlycosylated queuosines in tRNAs optimize translational rate and post-embryonic growth.
Journal, issue, pagesCell, Vol. 186, Issue 25, Page 5517-5535.e24, Year 2023
Publish dateDec 7, 2023
AuthorsXuewei Zhao / Ding Ma / Kensuke Ishiguro / Hironori Saito / Shinichiro Akichika / Ikuya Matsuzawa / Mari Mito / Toru Irie / Kota Ishibashi / Kimi Wakabayashi / Yuriko Sakaguchi / Takeshi Yokoyama / Yuichiro Mishima / Mikako Shirouzu / Shintaro Iwasaki / Takeo Suzuki / Tsutomu Suzuki /
PubMed AbstractTransfer RNA (tRNA) modifications are critical for protein synthesis. Queuosine (Q), a 7-deaza-guanosine derivative, is present in tRNA anticodons. In vertebrate tRNAs for Tyr and Asp, Q is further ...Transfer RNA (tRNA) modifications are critical for protein synthesis. Queuosine (Q), a 7-deaza-guanosine derivative, is present in tRNA anticodons. In vertebrate tRNAs for Tyr and Asp, Q is further glycosylated with galactose and mannose to generate galQ and manQ, respectively. However, biogenesis and physiological relevance of Q-glycosylation remain poorly understood. Here, we biochemically identified two RNA glycosylases, QTGAL and QTMAN, and successfully reconstituted Q-glycosylation of tRNAs using nucleotide diphosphate sugars. Ribosome profiling of knockout cells revealed that Q-glycosylation slowed down elongation at cognate codons, UAC and GAC (GAU), respectively. We also found that galactosylation of Q suppresses stop codon readthrough. Moreover, protein aggregates increased in cells lacking Q-glycosylation, indicating that Q-glycosylation contributes to proteostasis. Cryo-EM of human ribosome-tRNA complex revealed the molecular basis of codon recognition regulated by Q-glycosylations. Furthermore, zebrafish qtgal and qtman knockout lines displayed shortened body length, implying that Q-glycosylation is required for post-embryonic growth in vertebrates.
External linksCell / PubMed:37992713
MethodsEM (single particle)
Resolution2.26 - 2.67 Å
Structure data

33660

7y7c

EMDB-33660, PDB-7y7c:
Structure of the Bacterial Ribosome with human tRNA Asp(G34) and mRNA(GAU)
Method: EM (single particle) / Resolution: 2.51 Å

33661

7y7d

EMDB-33661, PDB-7y7d:
Structure of the Bacterial Ribosome with human tRNA Asp(Q34) and mRNA(GAU)
Method: EM (single particle) / Resolution: 2.58 Å

33662

7y7e

EMDB-33662, PDB-7y7e:
Structure of the Bacterial Ribosome with human tRNA Asp(ManQ34) and mRNA(GAU)
Method: EM (single particle) / Resolution: 2.41 Å

33663

7y7f

EMDB-33663, PDB-7y7f:
Structure of the Bacterial Ribosome with human tRNA Asp(ManQ34) and mRNA(GAC)
Method: EM (single particle) / Resolution: 2.43 Å

33664

7y7g

EMDB-33664, PDB-7y7g:
Structure of the Bacterial Ribosome with human tRNA Tyr(GalQ34) and mRNA(UAU)
Method: EM (single particle) / Resolution: 2.34 Å

33665

7y7h

EMDB-33665, PDB-7y7h:
Structure of the Bacterial Ribosome with human tRNA Tyr(GalQ34) and mRNA(UAC)
Method: EM (single particle) / Resolution: 2.51 Å

36178

8jdj

EMDB-36178, PDB-8jdj:
Structure of the Human cytoplasmic Ribosome with human tRNA Asp(Q34) and mRNA(GAU)
Method: EM (single particle) / Resolution: 2.5 Å

36179

8jdk

EMDB-36179, PDB-8jdk:
Structure of the Human cytoplasmic Ribosome with human tRNA Asp(ManQ34) and mRNA(GAU)
Method: EM (single particle) / Resolution: 2.26 Å

36180

8jdl

EMDB-36180, PDB-8jdl:
Structure of the Human cytoplasmic Ribosome with human tRNA Tyr(GalQ34) and mRNA(UAU) (non-rotated state)
Method: EM (single particle) / Resolution: 2.42 Å

36181

8jdm

EMDB-36181, PDB-8jdm:
Structure of the Human cytoplasmic Ribosome with human tRNA Tyr(GalQ34) and mRNA(UAU) (rotated state)
Method: EM (single particle) / Resolution: 2.67 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-GAL:
beta-D-galactopyranose

ChemComp-ZN:
Unknown entry

Source
  • escherichia coli (E. coli)
  • homo sapiens (human)
KeywordsRIBOSOME / tRNA modifications / decoding

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