de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  ATPase cycle of an archaeal chaperonin

Gutsche, I., Mihalache, O., & Baumeister, W. (2000). ATPase cycle of an archaeal chaperonin. Journal of Molecular Biology, 300(1), 187-196.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7169-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-716A-7
Genre: Journal Article
Alternative Title : J. Mol. Biol

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Gutsche, I., Author
Mihalache, O.1, Author              
Baumeister, W.1, Author              
Affiliations:
1External Organizations, escidoc:persistent22              

Content

show
hide
Free keywords: Allostery; Chaperonin; Protein folding; Thermosome; Atpase.; Group-ii chaperonin; In-vitro; Thermoplasma-acidophilum; Crystal-structure; Functional-characterization; Acidothermophilic archaeon; Homooligomeric complexes; Sulfolobus-solfataricus; Escherichia-coli; Alpha-chaperonin.; Molecular Biology & Genetics in Current Contents(R)/Life Sciences.
 Abstract: Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified by GroEL from Escherichia coli, and the group II chaperonins, which comprise archaeal thermosome and eukaryotic TRiC/CCT. Therefore, this study addresses the mechanism of interaction of adenine nucleotides with recombinant alpha-only and native alpha beta-thermosomes from Thermoplasma acidophilum acidophilum, which also enables us to analyze the role of the heterooligomeric composition of the natural thermosome. Although all subunits of the alpha-only thermosome seem to bind nucleotides tightly and independently, the native chaperonin has two different classes of ATP-binding sites. Furthermore, for the alpha-only thermosome, the steady-state ATPase rate is determined by the cleavage reaction itself, whereas, for the alpha beta-thermosome, the rate-limiting step is associated with a post-hydrolysis isomerisation into a non-covalent ADP*P-i species prior to the release of the gamma-phosphate group. After half-saturation with ATP, a negative cooperativity in hydrolysis is observed for both thermosomes. The effect of Mg2+ and K+ nucleotide cycling is documented. We conclude that archaeal chaperonins have unique allosteric properties and discuss them in the light of the mechanism established for the group I chaperonins. (C) 2000 Academic Press. [References: 52]

Details

show
hide
Language(s):
 Dates: 2000
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 318653
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 300 (1) Sequence Number: - Start / End Page: 187 - 196 Identifier: -