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Literature summary extracted from

  • Brueckner, F.; Armache, K.J.; Cheung, A.; Damsma, G.E.; Kettenberger, H.; Lehmann, E.; Sydow, J.; Cramer, P.
    Structure-function studies of the RNA polymerase II elongation complex (2009), Acta Crystallogr. Sect. D, 65, 112-120.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.6 TFIIS an RNA cleavage stimulatory factor TFIIS. TFIIS can rescue an arrested polymerase by creating a new RNA 3' end at the active site from which transcription can resume, mechanism, overview Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.6 in order to obtain an atomic model of the complete Pol II, atomic models of the core Pol II at 2.8 A resolution and of the additional heterodimeric subcomplex of subunits Rpb4 and Rpb7 at 2.3 A resolution are combined and refined against the diffraction data obtained from a holo-Pol II crystal at 3.8 A resolution, method optimization Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.6 469000
-
 core protein of Pol II Saccharomyces cerevisiae
2.7.7.6 512000
-
 holoenzyme complex of Pol II Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.6 nucleoside triphosphate + RNAn Saccharomyces cerevisiae template is DNA diphosphate + RNAn+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.6 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.6 additional information the enzyme also shows RNA-dependent RNA polymerase activity, EC 2.7.7.48, but slower and less processive than the DNA-dependent activity. During active transcription, Pol II must overcome intrinsic DNA-arrest sites, which are generally rich in A-T base pairs and pose a natural obstacle to transcription. At such sites, Pol II moves backwards along DNA and RNA, resulting in extrusion of the RNA 3' end through the polymerase pore beneath the active site and transcriptional arrest. The RNA cleavage stimulatory factor TFIIS can rescue an arrested polymerase by creating a new RNA 3' end at the active site from which transcription can resume, mechanism, overview Saccharomyces cerevisiae ?
-
 ?
2.7.7.6 nucleoside triphosphate + RNAn template is DNA Saccharomyces cerevisiae diphosphate + RNAn+1
-
 ?
2.7.7.6 nucleoside triphosphate + RNAn template is DNA, RNA translation process and mechanism of DNA-damage recognition by Pol II, detailed overview Saccharomyces cerevisiae diphosphate + RNAn+1
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.6 decamer core protein of Pol II Saccharomyces cerevisiae
2.7.7.6 dodecamer holoenzyme complex of Pol II Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.7.7.6 Pol II
-
 Saccharomyces cerevisiae
2.7.7.6 RNA polymerase II
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.7.7.6 physiological function Pol II is the eukaryotic enzyme that is responsible for transcribing all protein-coding genes into mRNA. The mRNA-transcription cycle can be divided into three stages: initiation, elongation and termination. During elongation, Pol II moves along a DNA template and synthesizes a complementary RNA chain in a processive manner Saccharomyces cerevisiae