English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Signal recognition particle prevents N-terminal processing of bacterial membrane proteins.

Ranjan, A., Mercier, E., Bhatt, A., & Wintermeyer, W. (2017). Signal recognition particle prevents N-terminal processing of bacterial membrane proteins. Nature Communications, 8: 15562. doi:10.1038/ncomms15562.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-5951-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-5955-D
Genre: Journal Article

Files

show Files
hide Files
:
2450872.pdf (Publisher version), 752KB
Name:
2450872.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
:
2450872_Suppl.pdf (Supplementary material), 196KB
Name:
2450872_Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Ranjan, A.1, Author              
Mercier, E.1, Author              
Bhatt, A., 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: Bacterial proteins are synthesized with an N-formylated amino-terminal methionine, and N-formylated peptides elicit innate-immunity responses against bacterial infections. However, the source of these formylated peptides is not clear, as most bacterial proteins are co-translationally deformylated by peptide deformylase. Here we develop a deformylation assay with translating ribosomes as substrates, to show that the binding of the signal recognition particle (SRP) to signal sequences in nascent proteins on the ribosome prevents deformylation, whereas deformylation of nascent proteins without signal sequence is not affected. Deformylation and its inhibition by SRP are not influenced by trigger factor, a chaperone that interacts with nascent chains on the ribosome. We propose that bacterial inner-membrane proteins, in particular those with N-out topology, can retain their N-terminal formyl group during cotranslational membrane insertion and supply formylated peptides during bacterial infections.

Details

show
hide
Language(s): eng - English
 Dates: 2017-05-18
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms15562
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: 6 Volume / Issue: 8 Sequence Number: 15562 Start / End Page: - Identifier: -