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Literature summary for 2.1.1.309 extracted from

  • Letoquart, J.; Huvelle, E.; Wacheul, L.; Bourgeois, G.; Zorbas, C.; Graille, M.; Heurgue-Hamard, V.; Lafontaine, D.L.
    Structural and functional studies of Bud23-Trm112 reveal 18S rRNA N7-G1575 methylation occurs on late 40S precursor ribosomes (2014), Proc. Natl. Acad. Sci. USA, 111, E5518-E5526.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structures of Bud23-Trm112 MTase complexes, overview Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D112A site-directed mutagenesis Saccharomyces cerevisiae
D112R site-directed mutagenesis, methylation inactive mutant Saccharomyces cerevisiae
D77A site-directed mutagenesis, methylation inactive mutant, 25% remaining S-adenosyl-L-methionine binding activity Saccharomyces cerevisiae
D94A site-directed mutagenesis Saccharomyces cerevisiae
D94R site-directed mutagenesis Saccharomyces cerevisiae
E18A site-directed mutagenesis Saccharomyces cerevisiae
I31W site-directed mutagenesis, methylation inactive mutant, 25% remaining S-adenosyl-L-methionine binding activity Saccharomyces cerevisiae
K21E/R27E site-directed mutagenesis, methylation inactive mutant Saccharomyces cerevisiae
M96A site-directed mutagenesis Saccharomyces cerevisiae
additional information protein levels and cell growth of mutants compared to wild-type, overview. Reconstitution of Dhr1-Bud23-Trm112 ternary complex by mixing Bud23-Trm112 with a 1.5 M excess of Dhr1[58-270] in 20 mM Tris·HCl, pH 7.5, 50 mM NaCl, 0.010 mM ZnCl2, 5 mM 2-mercaptoethanol Saccharomyces cerevisiae
S118E site-directed mutagenesis, methylation and S-adenosyl-L-methionine binding inactive mutant Saccharomyces cerevisiae
S118R site-directed mutagenesis, methylation and S-adenosyl-L-methionine binding inactive mutant Saccharomyces cerevisiae
W122A site-directed mutagenesis, methylation inactive mutant Saccharomyces cerevisiae
Y159A site-directed mutagenesis, methylation inactive mutant, 50% remaining S-adenosyl-L-methionine binding activity Saccharomyces cerevisiae
Y22A site-directed mutagenesis, methylation inactive mutant Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae Bud23-Trm112 interacts directly with the box C/D snoRNA U3-associated DEAH RNA helicase Dhr1 supposedly involved in central pseudoknot formation. Bud23–Trm112 might also contribute to controlling formation of this irreversible and dramatic structural reorganization essential to overall folding of small subunit rRNA ?
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S-adenosyl-L-methionine + guanine1575 in 18S rRNA Saccharomyces cerevisiae Bud23 is active in 18S rRNA N7G methylation as a heterodimer in a complex with Trm112. Trm112 is a small zinc finger protein that interacts with and activates three class I MTases in addition to Bud23. N7-methylguanosine introduced at position 1575 on 18S rRNA by Bud23-Trm112 is at a ridge forming a steric block between P- and E-site tRNAs. G1575 is coordinated by a network of conserved Bud23 residues, overview S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P25627
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Bud23-Trm112 interacts directly with the box C/D snoRNA U3-associated DEAH RNA helicase Dhr1 supposedly involved in central pseudoknot formation. Bud23–Trm112 might also contribute to controlling formation of this irreversible and dramatic structural reorganization essential to overall folding of small subunit rRNA Saccharomyces cerevisiae ?
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S-adenosyl-L-methionine + guanine1575 in 18S rRNA Bud23 is active in 18S rRNA N7G methylation as a heterodimer in a complex with Trm112. Trm112 is a small zinc finger protein that interacts with and activates three class I MTases in addition to Bud23. N7-methylguanosine introduced at position 1575 on 18S rRNA by Bud23-Trm112 is at a ridge forming a steric block between P- and E-site tRNAs. G1575 is coordinated by a network of conserved Bud23 residues, overview Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N7-methylguanine1575 in 18S rRNA
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Synonyms

Synonyms Comment Organism
BUD23
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Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information Bud23 and Trm112 interact through formation of a beta-zipper involving main-chain atoms, burying an important hydrophobic surface and stabilizing the complex. The structures reveal that the coactivator Trm112 undergoes an induced fit to accommodate its methyltransferase (MTase) partner, identification of Bud23 residues important for Bud23-Trm112 complex formation and recruitment to pre-ribosomes Saccharomyces cerevisiae
physiological function Bud23-Trm112 is required for efficient pre-rRNA processing steps leading to 18S rRNA synthesis and methylation of 18S rRNA at position G1575. Identification amd localization of Bud23–Trm112 contacts with precursor ribosomes. The essential helicase Dhr1 interacts directly with Bud23-Trm112, proposing a concerted action of these proteins in ribosome assembly. The methyltransferase activity of Bud23-Trm112 is required for pre-rRNA processing are disconnected in time. Though Bud23-Trm112 binds precursor ribosomes at an early nucleolar stage, m7G methylation occurs at a late step of small subunit biogenesis, implying specifically delayed catalytic activation. Bud23-Trm112 interacts directly with the box C/D snoRNA U3-associated DEAH RNA helicase Dhr1 supposedly involved in central pseudoknot formation suggesting that Bud23-Trm112 might also contribute to controlling formation of this irreversible and dramatic structural reorganization essential to overall folding of small subunit rRNA. Formation of the Bud23-Trm112 complex is required for efficient 18S rRNA maturation Saccharomyces cerevisiae