TRNA pseudouridine13 synthase

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tRNA pseudouridine13 synthase
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EC no. 5.4.99.27
CAS no. 430429-15-5
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tRNA pseudouridine13 synthase (EC 5.4.99.27, TruD, YgbO, tRNA PSI13 synthase, RNA:PSI-synthase Pus7p, Pus7p, RNA:pseudouridine-synthase Pus7p, Pus7 protein) is an enzyme with systematic name tRNA-uridine13 uracil mutase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

tRNA uridine13 tRNA pseudouridine13

Pseudouridine synthase TruD from Escherichia coli specifically acts on uridine13 in tRNA.

Related Research Articles

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In enzymology, a tRNA (uracil-5-)-methyltransferase is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">SMG6</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">PUS1</span> Protein-coding gene in the species Homo sapiens

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TRNA-dihydrouridine20 synthase (NAD(P)+) (EC 1.3.1.91, Dus2p, tRNA-dihydrouridine synthase 2) is an enzyme with systematic name tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction

Multisite-specific tRNA:(cytosine-C5)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytosine-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (pseudouridine54-N1)-methyltransferase (EC 2.1.1.257, TrmY, m1Psi methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA pseudouridine516 synthase (EC 5.4.99.19, 16S RNA pseudouridine516 synthase, 16S PsiI516 synthase, 16S RNA Psi516 synthase, RNA pseudouridine synthase RsuA, RsuA, 16S RNA pseudouridine 516 synthase) is an enzyme with systematic name 16S rRNA-uridine516 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine55 synthase is an enzyme with systematic name tRNA-uridine55 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine32 synthase is an enzyme with systematic name tRNA-uridine32 uracil mutase. This enzyme catalyses the following chemical reaction

23S rRNA pseudouridine746 synthase (EC 5.4.99.29, RluA, 23S RNA PSI746 synthase, 23S rRNA pseudouridine synthase, pseudouridine synthase RluA) is an enzyme with systematic name 23S rRNA-uridine746 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine31 synthase is an enzyme with systematic name tRNA-uridine31 uracil mutase. This enzyme catalyses the following chemical reaction

21S rRNA pseudouridine2819 synthase is an enzyme with systematic name 21S rRNA-uridine2819 uracil mutase. This enzyme catalyses the following chemical reaction

Mitochondrial tRNA pseudouridine27/28 synthase is an enzyme with systematic name mitochondrial tRNA-uridine27/28 uracil mutase. This enzyme catalyses the following chemical reaction

tRNA pseudouridine38/39 synthase is an enzyme with systematic name tRNA-uridine38/39 uracil mutase. This enzyme catalyses the following chemical reaction

In archaea like in eukaryotes, uridines in various RNAs are converted to pseudouridines by ribonucleoprotein complexes (RNPs) containing H/ACA sRNA. Because of their conserved function, these sRNAs are also called small "nucleolar" RNAs (snoRNA) like in eukaryotes, despite no nucleus is present in prokaryotes. By using various computational and experimental approaches in three Pyrococcus genomes seven H/ACA sRNAs and 15 pseudouridine (Ψ) resides on rRNA were identified. One H/ACA motif was shown to guide up to three distinct pseudouridylations. Atypical pseudouridine guide RNA features were identified in Pyrobaculum species. Lack of the conserved 3'-terminal ACA sequence and sometimes lack of 5' portion of the pseudouridylation pocket feature in few conserved Pyrobaculum H/ACA-like sRNAs. A study by Toffano-Nioche et al. proposes an unified structure/function model based on the common structural components in "Euryarchaeota" and Thermoproteota shared by H/ACA and H/ACA-like motifs.

References

  1. ↑ Ericsson UB, Nordlund P, Hallberg BM (May 2004). "X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold". FEBS Letters. 565 (1–3): 59–64. doi:10.1016/j.febslet.2004.03.085. PMID   15135053. S2CID   31602560.
  2. ↑ Chan CM, Huang RH (September 2009). "Enzymatic characterization and mutational studies of TruD--the fifth family of pseudouridine synthases". Archives of Biochemistry and Biophysics. 489 (1–2): 15–9. doi:10.1016/j.abb.2009.07.023. PMID   19664587.
  3. ↑ Kaya Y, Ofengand J (June 2003). "A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya". RNA. 9 (6): 711–21. doi:10.1261/rna.5230603. PMC   1370438 . PMID   12756329.
  4. ↑ Behm-Ansmant I, Urban A, Ma X, Yu YT, Motorin Y, Branlant C (November 2003). "The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a novel multisite-multisubstrate RNA:Psi-synthase also acting on tRNAs". RNA. 9 (11): 1371–82. doi:10.1261/rna.5520403. PMC   1287059 . PMID   14561887.
  5. ↑ Urban A, Behm-Ansmant I, Branlant C, Motorin Y (February 2009). "RNA sequence and two-dimensional structure features required for efficient substrate modification by the Saccharomyces cerevisiae RNA:{Psi}-synthase Pus7p" (PDF). The Journal of Biological Chemistry. 284 (9): 5845–58. doi: 10.1074/jbc.m807986200 . PMID   19114708. S2CID   19586610.
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