1887

Abstract

Proteasomes play key roles in a variety of eukaryotic cell functions, including translation, transcription, metabolism, DNA repair and cell-cycle control. The biological functions of these multicatalytic proteases in archaea, however, are poorly understood. In this study, was used as a model to determine the influence the proteasome-specific inhibitor -lactacystin--lactone (LL) has on archaeal proteome composition. Addition of 20–30 μM LL had a widespread effect on the proteome, with a 38–42 % increase in the number of 2-D gel electrophoresis (2-DE) protein spots, from an average of 627 to 1036 spots. Protein identities for 17 of the spots that were easily separated by 2-DE and unique and/or increased 2- to 14-fold in the LL-treated cells were determined by tandem mass spectrometry (MS/MS). These included protein homologues of the DJ-1/ThiJ family, mobilization of sulfur system, translation elongation factor EF-1 A, ribosomal proteins, tubulin-like FtsZ, divalent metal ABC transporter, dihydroxyacetone kinase DhaL, aldehyde dehydrogenase and 2-oxoacid decarboxylase E1. Based on these results, inhibition of proteasomes had a global influence on proteome composition, including proteins involved in central functions of the cell.

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2007-07-01
2022-01-21
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