mRNA Capping (Homo sapiens)

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1-45565nucleoplasmcytosolCBP20S-adenosylmethionineCapping complex (with freed 5'- GMP)nascent pre-mRNA transcriptGTPCapping complex (GpppN..)S-adenosylhomocysteineCapping complex (hydrolyzed)RNA Pol II with phosphorylated CTD: CE complexCE:Pol II CTD:Spt5 complexCapping complex (initial)RNA Polymerase II (phosphorylated):TFIIF:capped pre-mRNAphospho-Spt5OrthophosphateCapping complex (intermediate)TFIIHRNA (guanine-7-) methyltransferasePol II transcription complex with (ser5) phosphorylated CTD containing extruded transcript to +30capped pre-mRNA:CBC:RNA Pol II (phosphorylated) complexCap Binding Complex (CBC)RNA Pol II with phosphorylated CTD: CE complex with activated GTmRNA capping enzymeDNACBP80GDPmRNA capping factors


Description

The 5'-ends of all eukaryotic pre-mRNAs studied thus far are converted to cap structures. The cap is thought to influence splicing of the first intron, and is bound by 'cap-binding' proteins, CBP80 and CBP20, in the nucleus. The cap is important for translation initiation, and it also interacts with the poly(A)terminus, via proteins, resulting in circularization of the mRNA to facilitate multiple rounds of translation. The cap is also important for mRNA stability, protecting it from 5' to 3' nucleases, and is required for mRNA export to the cytoplasm.
The capping reaction usually occurs very rapidly on nascent transcripts; after the synthesis of only a few nucleotides by RNA polymerase II. The capping reaction involves the conversion of the 5'-end of the nascent transcript from a triphosphate to a diphosphate by a RNA 5'-triphosphatase, followed by the addition of a guanosine monophosphate by the mRNA guanylyltransferase, to form a 5'-5'-triphosphate linkage. This cap is then methylated by 2'-O-methyltransferases.

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Quality Tags

Ontology Terms

 

Bibliography

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  1. Mizumoto K, Kaziro Y.; ''Messenger RNA capping enzymes from eukaryotic cells.''; PubMed Europe PMC Scholia
  2. Rossignol M, Kolb-Cheynel I, Egly JM.; ''Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH.''; PubMed Europe PMC Scholia
  3. Glover-Cutter K, Kim S, Espinosa J, Bentley DL.; ''RNA polymerase II pauses and associates with pre-mRNA processing factors at both ends of genes.''; PubMed Europe PMC Scholia
  4. Narita T, Yung TM, Yamamoto J, Tsuboi Y, Tanabe H, Tanaka K, Yamaguchi Y, Handa H.; ''NELF interacts with CBC and participates in 3' end processing of replication-dependent histone mRNAs.''; PubMed Europe PMC Scholia
  5. Gonatopoulos-Pournatzis T, Cowling VH.; ''Cap-binding complex (CBC).''; PubMed Europe PMC Scholia
  6. Görnemann J, Kotovic KM, Hujer K, Neugebauer KM.; ''Cotranscriptional spliceosome assembly occurs in a stepwise fashion and requires the cap binding complex.''; PubMed Europe PMC Scholia
  7. Bentley D.; ''Coupling RNA polymerase II transcription with pre-mRNA processing.''; PubMed Europe PMC Scholia
  8. Schultz P, Fribourg S, Poterszman A, Mallouh V, Moras D, Egly JM.; ''Molecular structure of human TFIIH.''; PubMed Europe PMC Scholia
  9. Heidemann M, Hintermair C, Voß K, Eick D.; ''Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription.''; PubMed Europe PMC Scholia
  10. Schoenberg DR, Maquat LE.; ''Re-capping the message.''; PubMed Europe PMC Scholia
  11. Yamada-Okabe T, Doi R, Shimmi O, Arisawa M, Yamada-Okabe H.; ''Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme.''; PubMed Europe PMC Scholia
  12. Shatkin AJ, Manley JL.; ''The ends of the affair: capping and polyadenylation.''; PubMed Europe PMC Scholia
  13. Giglia-Mari G, Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W.; ''A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A.''; PubMed Europe PMC Scholia
  14. Tsukamoto T, Shibagaki Y, Niikura Y, Mizumoto K.; ''Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase.''; PubMed Europe PMC Scholia
  15. Buratowski S.; ''Progression through the RNA polymerase II CTD cycle.''; PubMed Europe PMC Scholia
  16. Giacometti S, Benbahouche NEH, Domanski M, Robert MC, Meola N, Lubas M, Bukenborg J, Andersen JS, Schulze WM, Verheggen C, Kudla G, Jensen TH, Bertrand E.; ''Mutually Exclusive CBC-Containing Complexes Contribute to RNA Fate.''; PubMed Europe PMC Scholia
  17. Proudfoot NJ, Furger A, Dye MJ.; ''Integrating mRNA processing with transcription.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114780view16:27, 25 January 2021ReactomeTeamReactome version 75
113225view11:29, 2 November 2020ReactomeTeamReactome version 74
112446view15:39, 9 October 2020ReactomeTeamReactome version 73
101352view11:23, 1 November 2018ReactomeTeamreactome version 66
100890view20:57, 31 October 2018ReactomeTeamreactome version 65
100431view19:32, 31 October 2018ReactomeTeamreactome version 64
99980view16:15, 31 October 2018ReactomeTeamreactome version 63
99534view14:52, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99171view12:42, 31 October 2018ReactomeTeamreactome version 62
93902view13:43, 16 August 2017ReactomeTeamreactome version 61
93475view11:24, 9 August 2017ReactomeTeamreactome version 61
86572view09:21, 11 July 2016ReactomeTeamreactome version 56
83238view10:27, 18 November 2015ReactomeTeamVersion54
76815view08:03, 17 July 2014ReactomeTeamFixed remaining interactions
76519view11:45, 16 July 2014ReactomeTeamFixed remaining interactions
76140view13:57, 11 June 2014AnweshaFixed url error
76128view10:42, 11 June 2014AnweshaModified description
75852view09:50, 11 June 2014ReactomeTeamRe-fixing comment source
75552view10:34, 10 June 2014ReactomeTeamReactome 48 Update
74907view13:43, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74551view08:35, 30 April 2014ReactomeTeamReactome46
44921view10:47, 6 October 2011MartijnVanIerselOntology Term : 'transcription pathway' added !
42079view21:55, 4 March 2011MaintBotAutomatic update
39887view05:55, 21 January 2011MaintBotNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
CBP20 ProteinP52298 (UniProt)
CBP80 ProteinQ09161 (UniProt)
CE:Pol II CTD:Spt5

complex

ComplexREACT_2332 (Reactome) Spt5 reacts with Guanyl Transferase (GT) of the capping enzyme (CE).
Cap Binding

Complex (CBC)

ComplexREACT_3884 (Reactome)
Capping complex

(GpppN..)

ComplexREACT_2312 (Reactome)
Capping complex

(hydrolyzed)

ComplexREACT_4969 (Reactome)
Capping complex

(initial)

ComplexREACT_4555 (Reactome)
Capping complex

(with freed 5'- GMP)

ComplexREACT_4741 (Reactome)
Capping complex

(intermediate)

ComplexREACT_3580 (Reactome)
DNA UnknownREACT_3913 (Reactome)
GDP Metabolite17552 (ChEBI)
GTP Metabolite15996 (ChEBI)
Orthophosphate Metabolite18367 (ChEBI)
Pol II transcription

complex with (ser5) phosphorylated CTD containing extruded transcript to +30

ComplexREACT_2595 (Reactome)
RNA (guanine-7-)

methyltransferase

ProteinO43148 (UniProt)
RNA Pol II with

phosphorylated CTD: CE complex

ComplexREACT_2371 (Reactome)
RNA Pol II with

phosphorylated CTD: CE complex with activated GT

ComplexREACT_3171 (Reactome)
RNA Polymerase II

(phosphorylated): TFIIF:capped pre- mRNA

ComplexREACT_3935 (Reactome)
S-

adenosylhomocysteine

Metabolite16680 (ChEBI)
S-adenosylmethionine Metabolite15414 (ChEBI)
TFIIH ComplexREACT_3832 (Reactome)
capped pre-mRNA:

CBC:RNA Pol II (phosphorylated) complex

ComplexREACT_3243 (Reactome)
mRNA capping

enzyme

ProteinO60942 (UniProt)
mRNA capping

factors

ComplexREACT_4925 (Reactome)
nascent pre-mRNA

transcript

UnknownREACT_5393 (Reactome)
phospho-Spt5 ProteinREACT_14075 (Reactome)

Annotated Interactions

No annotated interactions

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