Structural highlights
Function
[C4QZQ7_KOMPG] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU363031] [C4R4Y0_KOMPG] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] [A0A1B2JER8_PICPA] Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.[RuleBase:RU364033] [F2QPE6_KOMPC] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[PIRNR:PIRNR005586]
Publication Abstract from PubMed
In the early stage of transcription, eukaryotic RNA polymerase II (Pol II) exchanges initiation factors with elongation factors to form an elongation complex (EC) for processive transcription. Here, we report the structure of the Pol II EC bound with the basal elongation factors Spt4/5, Elf1, and TFIIS. Spt4/5 (the Spt4/Spt5 complex) and Elf1 modify a wide area of the Pol II surface. Elf1 bridges the Pol II central cleft, completing the "DNA entry tunnel" for downstream DNA. Spt4 and the Spt5 NGN and KOW1 domains encircle the upstream DNA, constituting a "DNA exit tunnel". The Spt5 KOW4 and KOW5 domains augment the "RNA exit tunnel", directing the exiting nascent RNA. Thus, the EC establishes a completely different transcription/regulation platform from that of the initiation complexes.
Structure of the complete elongation complex of RNA polymerase II with basal factors.,Ehara H, Yokoyama T, Shigematsu H, Yokoyama S, Shirouzu M, Sekine SI Science. 2017 Aug 3. pii: eaan8552. doi: 10.1126/science.aan8552. PMID:28775211[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ehara H, Yokoyama T, Shigematsu H, Yokoyama S, Shirouzu M, Sekine SI. Structure of the complete elongation complex of RNA polymerase II with basal factors. Science. 2017 Aug 3. pii: eaan8552. doi: 10.1126/science.aan8552. PMID:28775211 doi:http://dx.doi.org/10.1126/science.aan8552
