As promoter opening has been analyzed only in the S. cerevisiae this event is Inferred from the homologous pathway in yeast.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1", "Q9UKN8-1" ], "evidence": [ { "id": "R-HSA-112150", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-112150" } ] }, { "id": "R-HSA-112152", "name": "RNA Polymerase III Promoter Opening at Type 3 Promoters", "equation": "", "summary": "Pol III initiation complexes open the promoter spontaneously. Indeed, this is the general case for DNA-dependent RNA polymerases. Only pol II, with its requirement for TFIIH-directed and ATP-dependent promoter opening is exceptional. TFIIH introduces a layer of mechanism that is not in the repertoire of any other transcriptase. Thus, it is pol III-mediated transcription that is, from a mechanistic perspective, most directly comparable with archaeal and also bacterial transcription.
As promoter opening has been analyzed only in the S. cerevisiae this event is Inferred from the homologous pathway in yeast.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-112152", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-112152" } ] }, { "id": "R-HSA-112153", "name": "RNA Polymerase III Simple Start Sequence Initiation At Type 1 Promoters", "equation": "", "summary": "Transcription by pol III initiates at characteristic, simple start sequences. The universal core of these start sites is a pyrimidine-purine step, transcription initiating most frequently with ATP or GTP. This event is inferred from an event in Saccharomyces cerevisiae.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1", "Q9UKN8-1" ], "evidence": [ { "id": "R-HSA-112153", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-112153" } ] }, { "id": "R-HSA-112155", "name": "RNA Polymerase III Simple Start Sequence Initiation At Type 2 Promoters", "equation": "", "summary": "Transcription by pol III initiates at characteristic, simple start sequences. The universal core of these start sites is a pyrimidine-purine step, transcription initiating most frequently with ATP or GTP. This event is inferred from an event in Saccharomyces cerevisiae.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1", "Q9UKN8-1" ], "evidence": [ { "id": "R-HSA-112155", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-112155" } ] }, { "id": "R-HSA-112156", "name": "RNA Polymerase III Simple Start Sequence Initiation At Type 3 Promoters", "equation": "", "summary": "Transcription by pol III initiates at characteristic, simple start sequences. The universal core of these start sites is a pyrimidine-purine step, transcription initiating most frequently with ATP or GTP. This event is inferred from an event in Saccharomyces cerevisiae.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-112156", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-112156" } ] }, { "id": "R-HSA-113442", "name": "RNA Polymerase III Retractive RNase Activity at U-tract Pause Sites", "equation": "", "summary": "Productive transcription is accompanied by retractive RNase activity at U-tract pause sites and at the terminator. The principal cleavage products are dinucleotides, and they are produced in large stoichiometric excess over complete transcripts, despite the rapid overall rate of productive RNA chain elongation. This event is inferred from an event in Saccharomyces cerevisiae.", "cellular_location": "nucleoplasm", "input_participant_list": [ "R-ALL-113704" ], "output_participant_list": [ "R-ALL-112475", "R-ALL-30181" ], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-113442", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-113442" } ] }, { "id": "R-HSA-113446", "name": "Initiation of RNA Polymerase III Productive Transcription", "equation": "", "summary": "The transition from abortive to productive transcription may occur at bp +5. The primary transcripts of pol III-transcribed genes are short, ~90 to 120 nt for tRNA and 5s RNA genes (which constitute the great majority of products) and even the longest transcripts (e.g. the RNA of the signal recognition particles) are only ~500 nt. This event is inferred from an event in Saccharomyces cerevisiae.", "cellular_location": "nucleoplasm", "input_participant_list": [ "R-ALL-9757634", "R-ALL-111980" ], "output_participant_list": [ "R-ALL-111987" ], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-113446", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-113446" } ] }, { "id": "R-HSA-113449", "name": "RNA Polymerase III Transcriptional Pause at Terminator Sequence", "equation": "", "summary": "RNA Polymerase III terminates transcription at extremely simple sites, consistent with its role in producing small transcripts. These sites are essentially \\Tn\\ (in the non-transcribed strand).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-113449", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-113449" } ] }, { "id": "R-HSA-113451", "name": "Resumption of RNA Polymerase III Productive Transcription", "equation": "", "summary": "The principal cleavage products are dinucleotides, and they are produced in large stoichiometric excess over complete transcripts. Overall productive RNA chain elongation proceeds quite rapidly. This event is inferred from an event in Saccharomyces cerevisiae.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-113451", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-113451" } ] }, { "id": "R-HSA-113454", "name": "RNA Polymerase III Termination and release of transcribed RNA", "equation": "", "summary": "Efficient transcript production requires efficient release of RNA polymerase at the terminator; slow release at the terminator of a short transcription unit quickly becomes rate limiting for transcription at steady state. Although pol III autonomously recognizes sequence terminators, proteins that help to rapidly detach pol III from the terminator can affect the productivity of transcription if they eliminate termination as the rate-limiting step.
La, NF1 family proteins, PC4 and topoisomerase I have been proposed as accessory pol III transcription factors that facilitate multi-cycle transcription by hspol III, and are hence described as positive regulators of termination.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [ "R-ALL-112478", "R-ALL-113448", "R-HSA-83716" ], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-113454", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-113454" } ] }, { "id": "R-HSA-113705", "name": "RNA Polymerase III Productive Transcription", "equation": "", "summary": "The principal cleavage products are dinucleotides, and they are produced in large stoichiometric excess over complete transcripts. Overall productive RNA chain elongation proceeds quite rapidly. This event is inferred from an event in Saccharomyces cerevisiae.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-113705", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-113705" } ] }, { "id": "R-HSA-1964482", "name": "RNA polymerase III transcribes microbial dsDNA to dsRNA", "equation": "", "summary": "RNA polymerase III (POL III) was reported to sense and transcribe cytosolic AT-rich dsDNA into 5'-triphosphate poly(A-U) RNA in human and mouse cells. This dsRNA ligand in turn activated retinoic acid-inducible gene I (RIG-I) leading to production of type I interferon and activation of the transcription factor NF-kappaB (Chiu YH et al. 2009, Ablasser A et al. 2009). Knockdown of POL III expression by siRNA or inhibition of its enzymatic activity by specific chemical inhibitor ML-60218 prevented IFN beta induction in HEK293 cells stimulated with DNA viruses or poly(dA-dT) (Chiu YH et al. 2009, Ablasser A et al. 2009). Moreover, Pol-III inhibition blocked interferon induction by intracellular Legionella pneumophila bacteria [Chiu YH et al 2009].
This project represents cytosolic RNA polymerase III as a complex comprising 17 subunits, although the precise biochemical composition of the cytosolic holoenzyme complex which specifically recognizes AT-rich DNA is not yet known.", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1" ], "evidence": [ { "id": "R-HSA-1964482", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1964482" } ] }, { "id": "R-HSA-76056", "name": "Recruitment of RNA polymerase III to TFIIIB:TFIIIC:TFIIIA:Type 1 Promoter Complex", "equation": "", "summary": "Cross-linking experiments performed in the yeast system have shown that within the transcription initiation complex, eight RNA polymerase III subunits can be cross-linked to DNA (Bartholomew et al., 1993). The C34 subunit, which is known to be required specifically for transcription initiation but not elongation (Wang and Roeder, 1997; Werner et al., 1993), maps the furthest upstream of the transcription start site, in close proximity to Brf1-TFIIIB (Bartholomew et al., 1993). Indeed, this subunit interacts with Brf1 (Khoo et al., 1994; Werner et al., 1993). The figure illustrates this and other protein-protein contacts involving RNA polymerase III subunits and either TFIIIC or Brf1-TFIIIB subunits. The contacts identified with S. cerevisiae proteins are indicated by stippled arrows, those identified with human protein by solid arrows. Both the S. cerevisiae RNA polymerase III subunits C53 and ABC10a interact with Tfc4 ( 1999; Flores et al., 1999), and both C17 and C34 interact with Brf1. The human subunit RPC62 interacts with TIIIC63, and RPC39 with the TFIIIC subunits TFIIIC90 and TFIIIC63 (Hsieh et al., 1999a) and the Brf1-TFIIIB subunits Brf1 and TBP (Wang and Roeder, 1997). The contacts between RNA polymerase III and TFIIIC subunits are not absolutely required for transcription in vitro with the S. cerevisiae system, in which TFIIIC can be stripped from the DNA after assembly of TFIIIB without compromising transcription (Kassavetis et al., 1990) or, indeed, where transcription can be performed in the absence of TFIIIC on TATA box-containing promoters (Kassavetis et al., 1995). Nevertheless, they may contribute to the recruitment of RNA polymerase III in vivo.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O14802-1", "Q9NW08-1", "Q9UKN8-1" ], "evidence": [ { "id": "R-HSA-76056", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-76056" } ] }, { "id": "R-HSA-76060", "name": "RNA Polymerase III Promoter Opening at Type 1 Promoters", "equation": "", "summary": "Pol III initiation complexes open the promoter spontaneously. Indeed, this is the general case for DNA-dependent RNA polymerases. Only pol II, with its requirement for TFIIH-directed and ATP-dependent promoter opening is exceptional. TFIIH introduces a layer of mechanism that is not in the repertoire of any other transcriptase. Thus, it is pol III-mediated transcription that is, from a mechanistic perspective, most directly comparable with archaeal and also bacterial transcription.
As promoter opening has been analyzed only in the S. cerevisiae this event is Inferred from the homologous pathway in yeast.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O14802-1",
"Q9NW08-1",
"Q9UKN8-1"
],
"evidence": [
{
"id": "R-HSA-76060",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-76060"
}
]
},
{
"id": "R-HSA-83803",
"name": "Recruitment of RNA Polymerase III to TFIIIB:SNAPc:Type 3 Promoter Complex",
"equation": "",
"summary": "The binding of SNAPc to the PSE is stabilized not only by cooperative interactions with the Oct-1 POU domain, but also by cooperative interactions with TBP and Brf2 (Hinkley et al., 2003 ; Ma and Hernandez, 2002; Mittal and Hernandez, 1997). Moreover, Brf2, which cannot bind to DNA on its own, recognizes and stabilizes TBP bound to the TATA box (Cabart and Murphy, 2001; Cabart and Murphy, 2002; Ma and Hernandez, 2002). Thus, the U6 transcription initiation complex is stabilized by a complex network of protein-protein and protein-DNA interactions. Nothing is known, however, about how the complex recruits RNA polymerase III.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O14802-1",
"Q9NW08-1"
],
"evidence": [
{
"id": "R-HSA-83803",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-83803"
}
]
},
{
"id": "R-HSA-83805",
"name": "Recruitment of RNA Polymerase III to the TFIIIB:TFIIIC: Type 2 Promoter Complex",
"equation": "",
"summary": "At the beginning of this reaction, 1 molecule of 'TFIIIB:TFIIIC:Type 2 Promoter Complex', and 1 molecule of 'RNA Polymerase III Holoenzyme' are present. At the end of this reaction, 1 molecule of 'RNA Polymerase III:TFIIIB:TFIIIC:Type 2 Promoter Complex' is present.
This reaction takes place in the 'nucleus' (Hernandez 2002, Geiduschek and Kassavettis 2001).
",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O14802-1",
"Q9NW08-1",
"Q9UKN8-1"
],
"evidence": [
{
"id": "R-HSA-83805",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-83805"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-ALL-111980",
"participant_name": "elongating pre-RNA Pol III oligonucleotide [nucleoplasm]",
"crossref": [
{
"id": "33697",
"database": "ChEBI",
"url": ""
},
{
"id": "33697",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-111984",
"participant_name": "released pre-RNA Pol III oligonucleotide [nucleoplasm]",
"crossref": [
{
"id": "33697",
"database": "ChEBI",
"url": ""
},
{
"id": "33697",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-111987",
"participant_name": "elongating pre-RNA Pol III transcript [nucleoplasm]",
"crossref": [
{
"id": "33697",
"database": "ChEBI",
"url": ""
},
{
"id": "33697",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-112475",
"participant_name": "paused pre-RNA Pol III transcript [nucleoplasm]",
"crossref": [
{
"id": "33697",
"database": "ChEBI",
"url": ""
},
{
"id": "33697",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-112478",
"participant_name": "released pre-RNA Pol III transcript [nucleoplasm]",
"crossref": [
{
"id": "33697",
"database": "ChEBI",
"url": ""
},
{
"id": "33697",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-113448",
"participant_name": "Polymerase III gene DNA with a termination site [nucleoplasm]",
"crossref": [
{
"id": "61120",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-113704",
"participant_name": "elongating pre-RNA Pol III transcript plus 1 nucleotide [nucleoplasm]",
"crossref": [
{
"id": "33697",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-30181",
"participant_name": "NDP [nucleoplasm]",
"crossref": [
{
"id": "16862",
"database": "ChEBI",
"url": ""
},
{
"id": "C00454",
"database": "COMPOUND",
"url": ""
},
{
"id": "16862",
"database": "ChEBI",
"url": ""
},
{
"id": "C00454",
"database": "COMPOUND",
"url": ""
}
]
},
{
"participant_id": "R-ALL-9757634",
"participant_name": "NTP [nucleoplasm]",
"crossref": [
{
"id": "61557",
"database": "ChEBI",
"url": ""
},
{
"id": "61557",
"database": "ChEBI",
"url": ""
},
{
"id": "61557",
"database": "ChEBI",
"url": ""
},
{
"id": "61557",
"database": "ChEBI",
"url": ""
},
{
"id": "61557",
"database": "ChEBI",
"url": ""
},
{
"id": "61557",
"database": "ChEBI",
"url": ""
},
{
"id": "61557",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-HSA-83716",
"participant_name": "RNA Polymerase III Holoenzyme [nucleoplasm]",
"crossref": [
{
"id": "CPX-2393",
"database": "ComplexPortal",
"url": ""
}
]
}
],
"reaction_enzymes": [
{
"uniprot_ac": "A8JUY3",
"gene_name": "Polr3A",
"activity": [
{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
{
"id": "A8JUY3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/A8JUY3"
}
]
},
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{
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}
]
}
]
},
{
"uniprot_ac": "B2RXC6",
"gene_name": "Polr3a",
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{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
{
"id": "B2RXC6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/B2RXC6"
}
]
},
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"id": "B2RXC6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/B2RXC6"
}
]
}
]
},
{
"uniprot_ac": "D3ZV30",
"gene_name": "Polr3b",
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{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
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"id": "D3ZV30",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/D3ZV30"
}
]
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"id": "D3ZV30",
"database": "UniProtKB",
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}
]
}
]
},
{
"uniprot_ac": "D3ZYB6",
"gene_name": "Polrmt",
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{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
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"id": "D3ZYB6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/D3ZYB6"
}
]
},
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"database": "UniProtKB",
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}
]
}
]
},
{
"uniprot_ac": "D4A5A6",
"gene_name": "Polr2a",
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"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
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"id": "D4A5A6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/D4A5A6"
}
]
},
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"database": "UniProtKB",
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}
]
}
]
},
{
"uniprot_ac": "E9PTB6",
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{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
{
"id": "E9PTB6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/E9PTB6"
}
]
},
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"activity": "",
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"database": "UniProtKB",
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}
]
}
]
},
{
"uniprot_ac": "G3V8Y5",
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"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
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"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/G3V8Y5"
}
]
},
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}
]
}
]
},
{
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"gene_name": "POLRMT",
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{
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"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
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"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O00411"
}
]
},
{
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"activity": "",
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"id": "O00411",
"database": "UniProtKB",
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}
]
}
]
},
{
"uniprot_ac": "O14802",
"gene_name": "POLR3A",
"activity": [
{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
{
"id": "O14802",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O14802"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "",
"evidence": [
{
"id": "O14802",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O14802"
}
]
}
]
},
{
"uniprot_ac": "O35134",
"gene_name": "Polr1a",
"activity": [
{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
{
"id": "O35134",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O35134"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "",
"evidence": [
{
"id": "O35134",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O35134"
}
]
}
]
},
{
"uniprot_ac": "O54888",
"gene_name": "Polr1b",
"activity": [
{
"ec_number": "2.7.7.6",
"activity": "a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1).",
"evidence": [
{
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