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Proteasome function is dispensable under normal but not under heat shock conditions in Thermoplasma acidophilum
Author(s) -
Ruepp Andreas,
Eckerskorn Christoph,
Bogyo Matthew,
Baumeister Wolfgang
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00205-1
Subject(s) - thermoplasma acidophilum , proteasome , biology , proteolysis , biochemistry , yarrowia , heat shock protein , lactacystin , microbiology and biotechnology , proteasome inhibitor , enzyme , yeast , gene
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‐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 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 .