Publication details

Structure and dynamics of the RNAPII CTDsome with Rtt103

Authors

JASNOVIDOVA Olga KLUMPLER Tomáš KUBÍČEK Karel KALYNYCH Sergei PLEVKA Pavel ŠTEFL Richard

Year of publication 2017
Type Article in Periodical
Magazine / Source Proceeding of the National Academy of Sciences of the USA
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.pnas.org/content/114/42/11133.full
Doi http://dx.doi.org/10.1073/pnas.1712450114
Field Biophysics
Keywords CTDsome; SAXS; NMR; X ray; Rtt103; RNA Polymerase II
Attached files
Description RNA polymerase II (RNAPII) not only transcribes protein coding genes and many noncoding RNA, but also coordinates transcription and RNA processing. This coordination is mediated by a long C-terminal domain (CTD) of the largest RNAPII subunit, which serves as a binding platform for many RNA/protein-binding factors involved in transcription regulation. In this work, we used a hybrid approach to visualize the architecture of the full-length CTD in complex with the transcription termination factor Rtt103. Specifically, we first solved the structures of the isolated subcomplexes at high resolution and then arranged them into the overall envelopes determined at low resolution by small-angle X-ray scattering. The reconstructed overall architecture of the Rtt103–CTD complex reveals how Rtt103 decorates the CTD platform.
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