English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Converting GTP hydrolysis into motion: Versatile translational elongation factor G.

Rodnina, M. V., Peske, F., Peng, B. Z., Belardinelli, R., & Wintermeyer, W. (2019). Converting GTP hydrolysis into motion: Versatile translational elongation factor G. Biological Chemistry, (in press). doi:10.1515/hsz-2019-0313.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0005-0A4C-C Version Permalink: http://hdl.handle.net/21.11116/0000-0005-0A4E-A
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Rodnina, M. V.1, Author              
Peske, F.1, Author              
Peng, B. Z.1, Author              
Belardinelli, R.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: protein synthesis; reading frame maintenance; ribosome bypassing; ribosome recycling; translocation
 Abstract: Elongation factor G (EF-G) is a translational GTPase that acts at several stages of protein synthesis. Its canonical function is to catalyze tRNA movement during translation elongation, but it also acts at the last step of translation to promote ribosome recycling. Moreover, EF-G has additional functions, such as helping the ribosome to maintain the mRNA reading frame or to slide over non-coding stretches of the mRNA. EF-G has an unconventional GTPase cycle that couples the energy of GTP hydrolysis to movement. EF-G facilitates movement in the GDP-Pi form. To convert the energy of hydrolysis to movement, it requires various ligands in the A site, such as a tRNA in translocation, an mRNA secondary structure element in ribosome sliding, or ribosome recycling factor in post-termination complex disassembly. The ligand defines the direction and timing of EF-G-facilitated motion. In this review, we summarize recent advances in understanding the mechanism of EF-G action as a remarkable force-generating GTPase.

Details

show
hide
Language(s): eng - English
 Dates: 2019-10-30
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1515/hsz-2019-0313
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biological Chemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: (in press) Start / End Page: - Identifier: -