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Namehelp_outline
a 5'-end (N7-methyl 5'-triphosphoguanosine)-adenosine-phospho-ribonucleoside in mRNA
Identifier
RHEA-COMP:15693
Reactive part
help_outline
- Name help_outline a 5'-end (N7-methyl 5'-triphospho-guanosine)-adenosine-ribonucleotide residue Identifier CHEBI:144021 Charge -3 Formula C26H33N10O23P4R SMILEShelp_outline C1(=O)NC(=NC2=C1[N+](=CN2[C@@H]3O[C@H](COP(OP(OP(OC[C@H]4O[C@H]([C@@H]([C@@H]4OP(OC[C@H]5O[C@H]([C@@H]([C@@H]5O*)O)*)(=O)[O-])O)N6C7=C(C(=NC=N7)N)N=C6)(=O)[O-])(=O)[O-])(=O)[O-])[C@@H](O)[C@H]3O)C)N 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (N7-methyl 5'-triphospho-guanosine)-adenosine Identifier CHEBI:144023 Charge -2 Formula C21H27N10O17P3 InChIKeyhelp_outline QQOHNVHGNZYSBP-XPWFQUROSA-L SMILEShelp_outline C1(=O)NC(=NC2=C1[N+](=CN2[C@@H]3O[C@H](COP(OP(OP(OC[C@H]4O[C@H]([C@@H]([C@@H]4O)O)N5C6=C(C(=NC=N6)N)N=C5)(=O)[O-])(=O)[O-])(=O)[O-])[C@@H](O)[C@H]3O)C)N 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a 5'-end phospho-ribonucleoside in mRNA
Identifier
RHEA-COMP:15692
Reactive part
help_outline
- Name help_outline 5'-end ribonucleotide residue Identifier CHEBI:138282 Charge -2 Formula C5H7O7PR SMILEShelp_outline [C@@H]1(O[C@H]([C@@H]([C@@H]1O*)O)*)COP([O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 27 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:60884 | RHEA:60885 | RHEA:60886 | RHEA:60887 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Identification of a quality-control mechanism for mRNA 5'-end capping.
Jiao X., Xiang S., Oh C., Martin C.E., Tong L., Kiledjian M.
The 7-methylguanosine cap structure at the 5' end of eukaryotic messenger RNAs is a critical determinant of their stability and translational efficiency. It is generally believed that 5'-end capping is a constitutive process that occurs during mRNA maturation and lacks the need for a quality-contr ... >> More
The 7-methylguanosine cap structure at the 5' end of eukaryotic messenger RNAs is a critical determinant of their stability and translational efficiency. It is generally believed that 5'-end capping is a constitutive process that occurs during mRNA maturation and lacks the need for a quality-control mechanism to ensure its fidelity. We recently reported that the yeast Rai1 protein has pyrophosphohydrolase activity towards mRNAs lacking a 5'-end cap. Here we show that, in vitro as well as in yeast cells, Rai1 possesses a novel decapping endonuclease activity that can also remove the entire cap structure dinucleotide from an mRNA. This activity is targeted preferentially towards mRNAs with unmethylated caps in contrast to the canonical decapping enzyme, Dcp2, which targets mRNAs with a methylated cap. Capped but unmethylated mRNAs generated in yeast cells with a defect in the methyltransferase gene are more stable in a rai1-gene-disrupted background. Moreover, rai1Δ yeast cells with wild-type capping enzymes show significant accumulation of mRNAs with 5'-end capping defects under nutritional stress conditions of glucose starvation or amino acid starvation. These findings provide evidence that 5'-end capping is not a constitutive process that necessarily always proceeds to completion and demonstrates that Rai1 has an essential role in clearing mRNAs with aberrant 5'-end caps. We propose that Rai1 is involved in an as yet uncharacterized quality control process that ensures mRNA 5'-end integrity by an aberrant-cap-mediated mRNA decay mechanism. << Less
Nature 467:608-611(2010) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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A mammalian pre-mRNA 5' end capping quality control mechanism and an unexpected link of capping to pre-mRNA processing.
Jiao X., Chang J.H., Kilic T., Tong L., Kiledjian M.
Recently, we reported that two homologous yeast proteins, Rai1 and Dxo1, function in a quality control mechanism to clear cells of incompletely 5' end-capped messenger RNAs (mRNAs). Here, we report that their mammalian homolog, Dom3Z (referred to as DXO), possesses pyrophosphohydrolase, decapping, ... >> More
Recently, we reported that two homologous yeast proteins, Rai1 and Dxo1, function in a quality control mechanism to clear cells of incompletely 5' end-capped messenger RNAs (mRNAs). Here, we report that their mammalian homolog, Dom3Z (referred to as DXO), possesses pyrophosphohydrolase, decapping, and 5'-to-3' exoribonuclease activities. Surprisingly, we found that DXO preferentially degrades defectively capped pre-mRNAs in cells. Additional studies show that incompletely capped pre-mRNAs are inefficiently spliced at all introns, a fact that contrasts with current understanding, and are also poorly cleaved for polyadenylation. Crystal structures of DXO in complex with substrate mimic and products at a resolution of up to 1.5Å provide elegant insights into the catalytic mechanism and molecular basis for their three apparently distinct activities. Our data reveal a pre-mRNA 5' end capping quality control mechanism in mammalian cells, indicating DXO as the central player for this mechanism, and demonstrate an unexpected intimate link between proper 5' end capping and subsequent pre-mRNA processing. << Less
Mol. Cell 50:104-115(2013) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.