5.4.99.27: tRNA pseudouridine13 synthase
This is an abbreviated version!
For detailed information about tRNA pseudouridine13 synthase, go to the full flat file.
Word Map on EC 5.4.99.27
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5.4.99.27
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archaea
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rrna
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eukarya
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pseudouridylation
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pre-trnatyr
- 5.4.99.27
- archaea
- rrna
- eukarya
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pseudouridylation
- pre-trnatyr
Reaction
Synonyms
Pab aPus7, PSI, PUS7, Pus7 protein, Pus7p, RNA:pseudouridine-synthase Pus7p, RNA:PSI-synthase Pus7p, Sso aPus7, tRNA PSI13 synthase, TruD, YgbO
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General Information on EC 5.4.99.27 - tRNA pseudouridine13 synthase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
TruD folds into a V-shaped molecule with a catalytic domain that is structurally very similar to the catalytic modules of the other known pseudouridine synthases despite its lack of sequence homology and likely arose by divergent evolution
malfunction
metabolism
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Pus7p that catalyses U2 pseudouridylation at position 35, also catalyses pseudouridylation at position 56 during nutrient deprivation or heat shock
physiological function
additional information
transcriptome-wide quantitative mapping of Psi, method development using Psi-seq, relying on the unique stability of N3-[N-cyclohexyl-N'-beta-(4-methylmorpholinium)ethylcarbodiimide-Psi] (N3-CMC-Psi) to alkaline hydrolysis, and the ability of N3-CMC-Psi to terminate reverse transcription. For rRNA, 24/24 Cbf5-dependent sites are known targets of pseudouridylation, 8/9 associations between snoRNAs and rRNA sites are known, as is the identified Pus5-mediated Psi site in mitochondrial 21S rRNA. One snR3-dependent site at position 2140 on 25S rRNA is not specificated, detailed overview. Cbf5-dependent-Psi sites in mRNAs and snoRNAs are likely snoRNA-guided
malfunction
deletion of the ygbO gene causes the loss of tRNAGlu pseudouridine13 and plasmid-borne restoration of the structural gene restores pseudouridine13. Growth competition does not show any effect of the deletion
malfunction
disruption of the PUS7 gene abolishes pseudouridine13 formation in tRNAs in vivo. Absence of pseudouridine13 formation in tRNAAsp and tRNAGlu extracted from the DELTAPUS7 strain
malfunction
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using a Pus7p mutant strain it is shown that Pus7p is responsible for inducible U2 pseudouridylation at position 56
malfunction
PUS7 inactivation in embryonic stem cells impairs tRNA-derived small fragments (tRFs)-mediated translation regulation, leading to increased protein biosynthesis and defective germ layer specification. Dysregulation of this posttranscriptional regulatory circuitry impairs hematopoietic stem cell commitment and is common to aggressive subtypes of human myelodysplastic syndromes, overview. PUS7 loss impacts early embryogenesis and mesoderm specification
physiological function
pseudouridylation (Psi) is the most abundant and widespread type of RNA epigenetic modification in living organisms. Psi-driven posttranscriptional program steers translation control to impact stem cell commitment during early embryogenes. Mechanistically, the Psi writer PUS7 modifies and activates a network of tRNA-derived small fragments (tRFs) targeting the translation initiation complex. Critical function of Psi in directing translation control in stem cells with important implications for development and disease. PUS7 Psi synthase activity impacts stem cell size and protein biosynthesis. PUS7 binds specific tRNA isoacceptors in human stem cells, hESCs. PUS7-mediated Psi directs tRNA-derived small RNAs to inhibit translation. Psi is critically required for 5'tRF-dependent translational repression in vivo. Pseudouridylated mTOG targets the translation initiation complex. PUS7-mediated Psi critically governs hematopoietic stem cell function
physiological function
the most abundant RNA modification is pseudouridine (Psi), Psi is ubiquitous in diverse RNAs, and dynamic in mRNA. Pseudouridylation profiles and mechanisms. Pus7-dependent induction of pseudouridylation during heat shock
