+Search query
-Structure paper
Title | Molecular mechanism of promoter opening by RNA polymerase III. |
---|---|
Journal, issue, pages | Nature, Vol. 553, Issue 7688, Page 295-300, Year 2018 |
Publish date | Jan 17, 2018 |
Authors | Matthias K Vorländer / Heena Khatter / Rene Wetzel / Wim J H Hagen / Christoph W Müller / |
PubMed Abstract | RNA polymerase III (Pol III) and transcription factor IIIB (TFIIIB) assemble together on different promoter types to initiate the transcription of small, structured RNAs. Here we present structures ...RNA polymerase III (Pol III) and transcription factor IIIB (TFIIIB) assemble together on different promoter types to initiate the transcription of small, structured RNAs. Here we present structures of Pol III preinitiation complexes, comprising the 17-subunit Pol III and the heterotrimeric transcription factor TFIIIB, bound to a natural promoter in different functional states. Electron cryo-microscopy reconstructions, varying from 3.7 Å to 5.5 Å resolution, include two early intermediates in which the DNA duplex is closed, an open DNA complex, and an initially transcribing complex with RNA in the active site. Our structures reveal an extremely tight, multivalent interaction between TFIIIB and promoter DNA, and explain how TFIIIB recruits Pol III. Together, TFIIIB and Pol III subunit C37 activate the intrinsic transcription factor-like activity of the Pol III-specific heterotrimer to initiate the melting of double-stranded DNA, in a mechanism similar to that of the Pol II system. |
External links | Nature / PubMed:29345638 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.7 - 5.5 Å |
Structure data | EMDB-4181, PDB-6f41: EMDB-4182: RNA Polymerase III closed complex CC1 EMDB-4183: RNA Polymerase III closed complex CC2 EMDB-4184: |
Chemicals | ChemComp-ZN: |
Source |
|
Keywords | TRANSCRIPTION / RNA Polymerase III / TFIIIB / Pre-initiation complex / Brf1 / Bdp1 / TBP / Pol III / Enzyme / Closed complex |