English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Dual use of GTP hydrolysis by elongation factor G on the ribosome.

da Cunha, C. E. L., Belardinelli, R., Peske, F., Holtkamp, W., Wintermeyer, W., & Rodnina, M. V. (2013). Dual use of GTP hydrolysis by elongation factor G on the ribosome. Translation, 1(1): e24315. doi:10.4161/trla.24315.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-FB9B-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C82C-8
Genre: Journal Article

Files

show Files
hide Files
:
1740093.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
1740093.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
da Cunha, C. E. L.1, Author              
Belardinelli, R.1, Author              
Peske, F.1, Author              
Holtkamp, W.1, Author              
Wintermeyer, W.2, Author              
Rodnina, M. V.1, 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: Ribosomes, molecular motors, protein synthesis, tRNA, translational GTPases
 Abstract: Elongation factor G (EF-G) is a GTPase that catalyzes tRNA and mRNA translocation during the elongation cycle of protein synthesis. The GTP-bound state of the factor on the ribosome has been studied mainly with non-hydrolyzable analogs of GTP, which led to controversial conclusions about the role of GTP hydrolysis in translocation. Here we describe a mutant of EF-G in which the catalytic His91 is replaced with Ala. The mutant EF-G does not hydrolyze GTP, but binds GTP with unchanged affinity, allowing us to study the function of the authentic GTP-bound form of EF-G in translocation. Utilizing fluorescent reporter groups attached to the tRNAs, mRNA, and the ribosome we compile the velocity map of translocation seen from different perspectives. The data suggest that GTP hydrolysis accelerates translocation up to 30-fold and facilitates conformational rearrangements of both 30S subunit (presumably the backward rotation of the 30S head) and EF-G that lead to the dissociation of the factor. Thus, EF-G combines the energy regime characteristic for motor proteins, accelerating movement by a conformational change induced by GTP hydrolysis, with that of a switch GTPase, which upon Pi release switches the conformations of EF-G and the ribosome to low affinity, allowing the dissociation of the factor.

Details

show
hide
Language(s): eng - English
 Dates: 2013-04-012013-04
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.4161/trla.24315
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Translation
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 1 (1) Sequence Number: e24315 Start / End Page: - Identifier: -