English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Timing of GTP binding and hydrolysis by translation termination factor RF3.

Peske, F., Kuhlenkötter, S., Rodnina, M. V., & Wintermeyer, W. (2014). Timing of GTP binding and hydrolysis by translation termination factor RF3. Nucleic Acids Research, 42(3), 1812-1820. doi:10.1093/nar/gkt1095.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-A588-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CB83-8
Genre: Journal Article

Files

show Files
hide Files
:
1854610.pdf (Publisher version), 574KB
Name:
1854610.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Peske, F.1, Author              
Kuhlenkötter, S.1, Author              
Rodnina, M. V.1, Author              
Wintermeyer, W.2, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578599              

Content

show
hide
Free keywords: -
 Abstract: Protein synthesis in bacteria is terminated by release factors 1 or 2 (RF1/2), which, on recognition of a stop codon in the decoding site on the ribosome, promote the hydrolytic release of the polypeptide from the transfer RNA (tRNA). Subsequently, the dissociation of RF1/2 is accelerated by RF3, a guanosine triphosphatase (GTPase) that hydrolyzes GTP during the process. Here we show that—in contrast to a previous report—RF3 binds GTP and guanosine diphosphate (GDP) with comparable affinities. Furthermore, we find that RF3–GTP binds to the ribosome and hydrolyzes GTP independent of whether the P site contains peptidyl-tRNA (pre-termination state) or deacylated tRNA (post-termination state). RF3–GDP in either pre- or post-termination complexes readily exchanges GDP for GTP, and the exchange is accelerated when RF2 is present on the ribosome. Peptide release results in the stabilization of the RF3–GTP–ribosome complex, presumably due to the formation of the hybrid/rotated state of the ribosome, thereby promoting the dissociation of RF1/2. GTP hydrolysis by RF3 is virtually independent of the functional state of the ribosome and the presence of RF2, suggesting that RF3 acts as an unregulated ribosome-activated switch governed by its internal GTPase clock.

Details

show
hide
Language(s): eng - English
 Dates: 2013-11-082014-03
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1093/nar/gkt1095
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nucleic Acids Research
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 42 (3) Sequence Number: - Start / End Page: 1812 - 1820 Identifier: -