Enzymes
| UniProtKB help_outline | 4 proteins |
| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
queuosine34 in tRNATyr
Identifier
RHEA-COMP:19044
Reactive part
help_outline
- Name help_outline queuosine 5'-phosphate residue Identifier CHEBI:194431 Charge -1 Formula C17H21N5O9P Positionhelp_outline 34 SMILEShelp_outline C1(=O)NC(=NC2=C1C(=CN2[C@@H]3O[C@H](COP(*)([O-])=O)[C@@H](O*)[C@H]3O)CN[C@H]4C=C[C@@H]([C@@H]4O)O)N 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-α-D-galactose Identifier CHEBI:66914 Charge -2 Formula C15H22N2O17P2 InChIKeyhelp_outline HSCJRCZFDFQWRP-ABVWGUQPSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 124 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
O-5''-β-D-galactosylqueuosine34 in tRNATyr
Identifier
RHEA-COMP:19043
Reactive part
help_outline
- Name help_outline β-D-galactosyl-5''-O-queuosine 5'-phosphate residue Identifier CHEBI:228254 Charge -1 Formula C23H31N5O14P Positionhelp_outline 34 SMILEShelp_outline C1(=O)NC(=NC2=C1C(=CN2[C@@H]3O[C@H](COP(*)([O-])=O)[C@@H](O*)[C@H]3O)CN[C@H]4C=C[C@@H]([C@@H]4O[C@H]5[C@@H]([C@H]([C@H]([C@H](O5)CO)O)O)O)O)N 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 637 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:78231 | RHEA:78232 | RHEA:78233 | RHEA:78234 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| Gene Ontology help_outline |
Publications
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Glycosylated queuosines in tRNAs optimize translational rate and post-embryonic growth.
Zhao X., Ma D., Ishiguro K., Saito H., Akichika S., Matsuzawa I., Mito M., Irie T., Ishibashi K., Wakabayashi K., Sakaguchi Y., Yokoyama T., Mishima Y., Shirouzu M., Iwasaki S., Suzuki T., Suzuki T.
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 ... >> More
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. << Less
Cell 0:0-0(2023) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.