English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  DafA cycles between the DnaK chaperone system and translational machinery

Dumitru, G. L., Groemping, Y., Klostermeier, D., Restle, T., Deuerling, E., & Reinstein, J. (2004). DafA cycles between the DnaK chaperone system and translational machinery. Journal of Molecular Biology (London), 339(5), 1179-1189. doi:10.1016/j.jmb.2004.04.052.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : DafA cycles between the DnaK chaperone system and translational machinery

Files

show Files
hide Files
:
JMolBiol_339_2004_1179.pdf (Any fulltext), 434KB
 
File Permalink:
-
Name:
JMolBiol_339_2004_1179.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Dumitru, Georgeta L., Author
Groemping, Yvonne1, Author              
Klostermeier, Dagmar, Author
Restle, Tobias1, Author              
Deuerling, Elke, Author
Reinstein, Jochen1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: chaperone; heat shock; ribosome; folding; regulation
 Abstract: DafA is encoded by the dnaK operon of Thermus thermophilus and mediates the formation of a highly stable complex between the chaperone DnaK and its co-chaperone DnaJ under normal growth conditions. DafA(Tth) contains 87 amino acid residues and is the only member of the DnaK(Tth) chaperone system for which no corresponding protein has yet been identified in other organisms and whose particular function has remained elusive. Here, we show directly that the DnaK(Tth)-DnaJ(Tth)-DafA(Tth) complex cannot represent the active chaperone species since DafA(Tth) inhibits renaturation of firefly luciferase by suppressing substrate association. Since DafA(Tth) must be released before the substrate proteins can bind we hypothesized that free DafA(Tth) might have regulatory functions connected to the heat shock response. Here, we present evidence that supports this hypothesis. We identified the 70S ribosome as binding target of free DafA(Tth). Our results show that the association of DafA(Tth) and 70S ribosomes does not require the participation of DnaK(Tth) or DnaJ(Tth). On the contrary, the assembly of DnaK(Tth)-DnaJ(Tth)-DafA(Tth) and ribosome-DafA(Tth) complexes seems to be competitive. These findings strongly suggest the involvement of DafA(Tth) in regulatory processes occurring at a translational level, which could represent a new mechanism of heat shock response as an adaptation to elevated temperature.

Details

show
hide
Language(s): eng - English
 Dates: 2004-04-202004-02-232004-04-212004-05-112004-06-18
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Academic Press
Pages: - Volume / Issue: 339 (5) Sequence Number: - Start / End Page: 1179 - 1189 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042