English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity

Beinker, P., Schlee, S., Groemping, Y., Seidel, R., & Reinstein, J. (2002). The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity. The Journal of Biological Chemistry, 277(49), 47160-47166. doi:10.1074/jbc.M207853200.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity

Files

show Files
hide Files
:
JBiolChem_277_2002_47160.pdf (Any fulltext), 161KB
 
File Permalink:
-
Name:
JBiolChem_277_2002_47160.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Beinker, Philipp1, Author           
Schlee, Sandra1, Author           
Groemping, Yvonne1, Author           
Seidel, Ralf, 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: -
 Abstract: ClpB from Thermus thermophilus belongs to the Clp/Hsp100 protein family and reactivates protein aggregates in cooperation with the DnaK chaperone system. The mechanism of protein reactivation and interaction with the DnaK system remains unclear. ClpB possesses two nucleotide binding domains, which are essential for function and show a complex allosteric behavior. The role of the N-terminal domain that precedes the first nucleotide binding domain is largely unknown. We purified and characterized an N-terminal shortened ClpB variant (ClpBDeltaN; amino acids 140-854), which remained active in refolding assays with three different substrate proteins. In addition the N-terminal truncation did not significantly change the nucleotide binding affinities, the nucleotide-dependent oligomerization, and the allosteric behavior of the protein. In contrast casein binding and stimulation of the ATPase activity by kappa-casein were affected. These results suggest that the N-terminal domain is not essential for the chaperone function, does not influence the binding of nucleotides, and is not involved in the formation of intermolecular contacts. It contributes to the casein binding site of ClpB, but other substrate proteins do not necessarily interact with the N terminus. This indicates a substantial difference in the binding mode of kappa-casein that is often used as model substrate for ClpB and other possibly more suitable substrate proteins.

Details

show
hide
Language(s): eng - English
 Dates: 2002-08-022002-09-252002-09-252002-12-06
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665815
DOI: 10.1074/jbc.M207853200
URI: http://www.ncbi.nlm.nih.gov/pubmed/12351638
Other: 6063
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 277 (49) Sequence Number: - Start / End Page: 47160 - 47166 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1