Enzymes
| UniProtKB help_outline | 8,753 proteins |
Reaction participants Show >> << Hide
-
Namehelp_outline
a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA
Identifier
RHEA-COMP:16801
Reactive part
help_outline
- Name help_outline G5'ppp5'm2'AACA-mRNA Identifier CHEBI:156482 Charge -6 Formula C51H59N22O36P6 SMILEShelp_outline C1(=O)NC(=NC2=C1N=CN2[C@@H]3O[C@H](COP(OP(OP(=O)([O-])OC[C@H]4O[C@@H](N5C=6N=CN=C(N)C6N=C5)[C@@H]([C@@H]4OP(OC[C@H]7O[C@@H](N8C=9N=CN=C(N)C9N=C8)[C@@H]([C@@H]7OP(OC[C@H]%10O[C@@H](N%11C(NC(=O)C(=C%11)C)=O)[C@@H]([C@@H]%10OP(OC[C@H]%12O[C@@H](N%13C=%14N=CN=C(N)C%14N=C%13)[C@@H]([C@@H]%12*)O)(=O)[O-])O)(=O)[O-])O)(=O)[O-])OC)(=O)[O-])(=O)[O-])[C@@H](O)[C@H]3O)N 2D coordinates Mol file for the small molecule Search links Involved in 2 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 842 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA
Identifier
RHEA-COMP:16798
Reactive part
help_outline
- Name help_outline m7G5'ppp5'm2'AACA-mRNA Identifier CHEBI:156483 Charge -5 Formula C52H62N22O36P6 SMILEShelp_outline C1(=O)NC(=NC2=C1[N+](=CN2[C@@H]3O[C@H](COP(OP(OP(=O)([O-])OC[C@H]4O[C@@H](N5C=6N=CN=C(N)C6N=C5)[C@@H]([C@@H]4OP(OC[C@H]7O[C@@H](N8C=9N=CN=C(N)C9N=C8)[C@@H]([C@@H]7OP(OC[C@H]%10O[C@@H](N%11C(NC(=O)C(=C%11)C)=O)[C@@H]([C@@H]%10OP(OC[C@H]%12O[C@@H](N%13C=%14N=CN=C(N)C%14N=C%13)[C@@H]([C@@H]%12*)O)(=O)[O-])O)(=O)[O-])O)(=O)[O-])OC)(=O)[O-])(=O)[O-])[C@@H](O)[C@H]3O)C)N 2D coordinates Mol file for the small molecule Search links Involved in 2 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 768 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:65440 | RHEA:65441 | RHEA:65442 | RHEA:65443 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Publications
-
Ribose 2'-O methylation of the vesicular stomatitis virus mRNA cap precedes and facilitates subsequent guanine-N-7 methylation by the large polymerase protein.
Rahmeh A.A., Li J., Kranzusch P.J., Whelan S.P.
During conventional mRNA cap formation, two separate methyltransferases sequentially modify the cap structure, first at the guanine-N-7 (G-N-7) position and subsequently at the ribose 2'-O position. For vesicular stomatitis virus (VSV), a prototype of the nonsegmented negative-strand RNA viruses, ... >> More
During conventional mRNA cap formation, two separate methyltransferases sequentially modify the cap structure, first at the guanine-N-7 (G-N-7) position and subsequently at the ribose 2'-O position. For vesicular stomatitis virus (VSV), a prototype of the nonsegmented negative-strand RNA viruses, the two methylase activities share a binding site for the methyl donor S-adenosyl-l-methionine and are inhibited by individual amino acid substitutions within the C-terminal domain of the large (L) polymerase protein. This led to the suggestion that a single methylase domain functions for both 2'-O and G-N-7 methylations. Here we report a trans-methylation assay that recapitulates both ribose 2'-O and G-N-7 modifications by using purified recombinant L and in vitro-synthesized RNA. Using this assay, we demonstrate that VSV L typically modifies the 2'-O position of the cap prior to the G-N-7 position and that G-N-7 methylation is diminished by pre-2'-O methylation of the substrate RNA. Amino acid substitutions in the C terminus of L that prevent all cap methylation in recombinant VSV (rVSV) partially retain the ability to G-N-7 methylate a pre-2'-O-methylated RNA, therefore uncoupling the effect of substitutions in the C terminus of the L protein on the two methylations. In addition, we show that the 2'-O and G-N-7 methylase activities act specifically on RNA substrates that contain the conserved elements of a VSV mRNA start at the 5' terminus. This study provides new mechanistic insights into the mRNA cap methylase activities of VSV L, demonstrates that 2'-O methylation precedes and facilitates subsequent G-N-7 methylation, and reveals an RNA sequence and length requirement for the two methylase activities. We propose a model of regulation of the activity of the C terminus of L protein in 2'-O and G-N-7 methylation of the cap structure. << Less
J. Virol. 83:11043-11050(2009) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
RHEA:65440 part of RHEA:65376