English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Structural basis for λN-dependent processive transcription antitermination.

Said, N., Krupp, F., Anedchenko, E., Santos, K. F., Dybkov, O., Huang, Y. H., et al. (2017). Structural basis for λN-dependent processive transcription antitermination. Nature Microbiology, 2: 2:17062. doi:10.1038/nmicrobiol.2017.62.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-244E-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-244F-A
Genre: Journal Article

Files

show Files
hide Files
:
Said.pdf (Publisher version), 7MB
Name:
Said.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
© 2017 Macmillan Publishers Limited, part of Springer Nature
License:
-

Locators

show

Creators

show
hide
 Creators:
Said, N., Author
Krupp, F., Author
Anedchenko, E., Author
Santos, K. F., Author
Dybkov, O., Author
Huang, Y. H., Author
Lee, C. T., Author
Loll, B., Author
Behrmann, E., Author
Buerger, J.1, 2, Author              
Mielke, T.1, Author              
Loerke, J., Author
Urlaub, H., Author
Spahn, C. M. T., Author
Weber, G., Author
Wahl, M. C., Author
Affiliations:
1Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
2Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: λN-mediated processive antitermination constitutes a paradigmatic transcription regulatory event, during which phage protein λN, host factors NusA, NusB, NusE and NusG, and an RNA nut site render elongating RNA polymerase termination-resistant. The structural basis of the process has so far remained elusive. Here we describe a crystal structure of a λN–NusA–NusB–NusE–nut site complex and an electron cryo-microscopic structure of a complete transcription antitermination complex, comprising RNA polymerase, DNA, nut site RNA, all Nus factors and λN, validated by crosslinking/mass spectrometry. Due to intrinsic disorder, λN can act as a multiprotein/RNA interaction hub, which, together with nut site RNA, arranges NusA, NusB and NusE into a triangular complex. This complex docks via the NusA N-terminal domain and the λN C-terminus next to the RNA exit channel on RNA polymerase. Based on the structures, comparative crosslinking analyses and structure-guided mutagenesis, we hypothesize that λN mounts a multipronged strategy to reprogram the transcriptional machinery, which may include (1) the λN C terminus clamping the RNA exit channel, thus stabilizing the DNA:RNA hybrid; (2) repositioning of NusA and RNAP elements, thus redirecting nascent RNA and sequestering the upstream branch of a terminator hairpin; and (3) hindering RNA engagement of termination factor ρ and/or obstructing ρ translocation on the transcript.

Details

show
hide
Language(s): eng - English
 Dates: 2017-04-28
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1038/nmicrobiol.2017.62
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Microbiology
  Abbreviation : Nat. Microbiol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London, UK : Nature Publishing Group
Pages: 13 Volume / Issue: 2 Sequence Number: 2:17062 Start / End Page: - Identifier: Other: 2058-5276
CoNE: https://pure.mpg.de/cone/journals/resource/2058-5276