English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Protein elongation, co-translational folding and targeting.

Rodnina, M. V., & Wintermeyer, W. (2016). Protein elongation, co-translational folding and targeting. Journal of Molecular Biology, 428(10, P. B), 2165-2185. doi:10.1016/j.jmb.2016.03.022.

Item is

Files

show Files
hide Files
:
2269445.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
2269445.pdf
Description:
-
OA-Status:
Visibility:
Restricted (UNKNOWN id 303; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:

Creators

show
hide
 Creators:
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: membrane targeting; protein folding; recoding; ribosome; translation factors
 Abstract: The elongation phase of protein synthesis defines the overall speed and fidelity of protein synthesis and affects protein folding and targeting. The mechanisms of reactions taking place during translation elongation remain important questions in understanding ribosome function. The ribosome-guided by signals in the mRNA-can recode the genetic information, resulting in alternative protein products. Co-translational protein folding and interaction of ribosomes and emerging polypeptides with associated protein biogenesis factors determine the quality and localization of proteins. In this review, we summarize recent findings on mechanisms of translation elongation in bacteria, including decoding and recoding, peptide bond formation, tRNA-mRNA translocation, co-translational protein folding, interaction with protein biogenesis factors and targeting of ribosomes synthesizing membrane proteins to the plasma membrane. The data provide insights into how the ribosome shapes composition and quality of the cellular proteome.

Details

show
hide
Language(s): eng - English
 Dates: 2016-03-302016-05-22
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jmb.2016.03.022
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Molecular Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 428 (10, P. B) Sequence Number: - Start / End Page: 2165 - 2185 Identifier: -