Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
guanosine2922 in 27S pre-rRNA
Identifier
RHEA-COMP:10200
Reactive part
help_outline
- Name help_outline GMP residue Identifier CHEBI:74269 Charge -1 Formula C10H11N5O7P Positionhelp_outline 2922 SMILEShelp_outline C1(=O)NC(=NC2=C1N=CN2[C@@H]3O[C@H](COP(=O)(*)[O-])[C@@H](O*)[C@H]3O)N 2D coordinates Mol file for the small molecule Search links Involved in 42 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 904 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
2'-O-methylguanosine2922 in 27S pre-rRNA
Identifier
RHEA-COMP:10201
Reactive part
help_outline
- Name help_outline 2'-O-methylguanosine 5'-phosphate residue Identifier CHEBI:74445 Charge -1 Formula C11H13N5O7P Positionhelp_outline 2922 SMILEShelp_outline C1(=O)NC(=NC2=C1N=CN2[C@@H]3O[C@H](COP(=O)(*)[O-])[C@@H](O*)[C@H]3OC)N 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 827 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 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:42724 | RHEA:42725 | RHEA:42726 | RHEA:42727 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2'-O-ribose methylation of a conserved rRNA position in yeast.
Bonnerot C., Pintard L., Lutfalla G.
In yeast, guide snoRNAs have been assigned to 51 of the 55 rRNA ribose methylation sites. LSU-Um2918 is one of the four remaining positions. This residue is highly conserved and located in the peptidyl transferase center of the ribosome. The equivalent position on the E. coli 23S rRNA is methylate ... >> More
In yeast, guide snoRNAs have been assigned to 51 of the 55 rRNA ribose methylation sites. LSU-Um2918 is one of the four remaining positions. This residue is highly conserved and located in the peptidyl transferase center of the ribosome. The equivalent position on the E. coli 23S rRNA is methylated by FtsJ/RrmJ which has three yeast homologs: Spb1, involved in biogenesis of LSU; Trm7, a tRNA methyltransferase; and Mrm2, a mitochondrial 21S rRNA methyltransferase. We demonstrate that a point mutation in the Ado-Met binding site of Spb1p affects cell growth but does not abolish methylation of U2918. When this mutation is combined with disruption of snR52 (a snoRNA C/D), cell growth is severely impaired and U2918 is no longer methylated. In vitro, Spb1p is able to methylate U2918 on 60S subunits. Our results reveal the importance of this methylation for which two mechanisms coexist: a site-specific methyltransferase (Spb1p) and a snoRNA-dependent mechanism. << Less
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Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage.
Lapeyre B., Purushothaman S.K.
rRNA molecules undergo extensive posttranscriptional modification, predominantly 2'-O-ribose methylation and pseudouridine formation, both of which are guided by the numerous small nucleolar RNAs in eukaryotes. Here, we describe an exception to this rule. The essential yeast nucleolar protein Spb1 ... >> More
rRNA molecules undergo extensive posttranscriptional modification, predominantly 2'-O-ribose methylation and pseudouridine formation, both of which are guided by the numerous small nucleolar RNAs in eukaryotes. Here, we describe an exception to this rule. The essential yeast nucleolar protein Spb1p is a site-specific rRNA methyltransferase modifying the universally conserved G2922 that is located within the A loop of the catalytic center of the ribosome. The equivalent position in bacteria is the docking site for aminoacyl-tRNA, and it is critical for translation. In sharp contrast to other 2'-O-methylriboses that are formed on the primary transcript, Gm2922 appears at a late processing stage, during the maturation of the 27S pre-rRNA. Thus, eukaryotes have maintained a site-specific enzyme to catalyze the methylation of a nucleotide that plays a crucial role in ribosome biogenesis and translation. << Less
Comments
Guanosine(2922) is a universally conserved position of the catalytic center of the ribosome that is essential for translation. 2'-O-methylguanosine(2922) is formed during the maturation of the 27S pre-rRNA.