English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Proteasome function is dispensable under normal but not under heat shock conditions in thermoplasma acidophilum

Ruepp, A., Eckerskorn, C., Bogyo, M., & Baumeister, W. (1998). Proteasome function is dispensable under normal but not under heat shock conditions in thermoplasma acidophilum. FEBS Letters, 425(1), 87-90.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Ruepp, A.1, Author              
Eckerskorn, C.1, Author              
Bogyo, M., Author
Baumeister, W.1, Author              
Affiliations:
1External Organizations, ou_persistent22              

Content

show
hide
Free keywords: Proteasome; Inhibitor; Thermoplasma acidophilum; Archaea.; Degradation; Inhibitors.; Biochemistry & biophysics.
 Abstract: Hitherto the biology of proteolysis in prokaryotes, particularly in archaea, is only poorly understood. We hale used the tri-peptide vinyl sulfone inhibitor carboxybenzyl-leucyl-leucyl-leucine vinyl sulfone (Z-L-3 VS) to study the in vivo function of proteasomes in Thermoplasma acidophilum. Z-L-3 VS is a potent inhibitor of the Thermoplasma proteasome and is capable of modifying 75 to 80% of the proteasomal beta-subunits in cell cultures. Inhibition of proteasomes has only marginal effects under normal growth conditions. Under heat shock conditions, however, the effects of proteasome inhibition are much more severe, to the extent of complete cell growth arrest. These data suggest that other proteolytic systems may exist that can compensate for the loss of proteasome function in T. acidophilum. (C) 1998 Federation of European Biochemical Societies. [References: 25]

Details

show
hide
Language(s):
 Dates: 1998-03-20
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 318415
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: FEBS Letters
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 425 (1) Sequence Number: - Start / End Page: 87 - 90 Identifier: -