English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Single-molecule tracking of mRNA exiting from RNA polymerase II.

Andrecka, J., Lewis, R., Brückner, F., Lehmann, E., Cramer, P., & Michaelis, J. (2008). Single-molecule tracking of mRNA exiting from RNA polymerase II. Proceedings of the National Academy of Sciences of the United States of America, 105(1), 135-140. doi:10.1073/pnas.0703815105.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-7F4C-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-8151-0
Genre: Journal Article

Files

show Files
hide Files
:
1936358.pdf (Publisher version), 832KB
Name:
1936358.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://www.pnas.org/content/105/1/135.full (Publisher version)
Description:
-

Creators

show
hide
 Creators:
Andrecka, J., Author
Lewis, R., Author
Brückner, F., Author
Lehmann, E., Author
Cramer, P.1, Author              
Michaelis, J., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

Content

show
hide
Free keywords: Pol II; transcription; FRET; triangulation; fluorescence
 Abstract: Single-pair fluorescence resonance energy transfer was used to track RNA exiting from RNA polymerase II (Pol II) in elongation complexes. Measuring the distance between the RNA S' end and three known locations within the elongation complex allows us determine its position by means of triangulation. RNA leaves the polymerase active center cleft via the previously proposed exit tunnel and then disengages from the enzyme surface. When the RNA reaches lengths of 26 and 29 nt, its 5' end associates with Pol 11 at the base of the dock domain. Because the initiation factor TFIIB binds to the dock domain and exit tunnel, exiting RNA may prevent TFIIB reassociation during elongation. RNA further extends toward the linker connecting to the polymerase C-terminal repeat domain (CTD), which binds the 5'-capping enzyme and other RNA processing factors.

Details

show
hide
Language(s): eng - English
 Dates: 2008-01-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.0703815105
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: National Academy of Sciences
Pages: - Volume / Issue: 105 (1) Sequence Number: - Start / End Page: 135 - 140 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230