Proteasome function is dispensable under normal but not under heat shock conditions in Thermoplasma acidophilum

FEBS Letters

Eckerskorn, Christoph²  Baumeister, Wolfgang²  Bogyo, Matthew¹  Ruepp, Andreas² 

[1] Department of Pathology, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115, USA;Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany

关键词: Proteasome;    Inhibitor;    Thermoplasma acidophilum;    Archaea;    OD;    optical density;    DMSO;    dimethyl sulfoxide;    NMec;    7-amino-4-methycoumarin;    Suc;    succinyl;   

DOI  :  10.1016/S0014-5793(98)00205-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hitherto the biology of proteolysis in prokaryotes, particularly in archaea, is only poorly understood. We have used the tri-peptide vinyl sulfone inhibitor carboxybenzyl-leucyl-leucyl-leucine vinyl sulfone (Z-L₃VS) to study the in vivo function of proteasomes in Thermoplasma acidophilum. Z-L₃VS is a potent inhibitor of the Thermoplasma proteasome and is capable of modifying 75 to 80% of the proteasomal β-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.

【 授权许可】

Unknown