The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-ring. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit. Here we report that the base subassembly of… (More)
We have developed a screening technology for the identification of short-lived proteins. A green fluorescent protein (GFP)-fusion cDNA library was generated for monitoring degradation kinetics. Cells expressing a subset of the GFP-cDNA expression library were screened to recover those in which the fluorescence signal diminished rapidly when protein… (More)
MOTIVATION The antizymes (AZ) are proteins that regulate cellular polyamine pools in metazoa. To search for remote homologs in single-celled eukaryotes, we used computer software based on hidden Markov models. The most divergent homolog detected was that of the fission yeast Schizosaccharomyces pombe. Sequence identities between S.POMBE: AZ and known AZs… (More)
The ubiquitin-proteasome system is the major degradation pathway for short-lived proteins in eukaryotic cells. Targets of the ubiquitin-proteasome-system are proteins regulating a broad range of cellular processes including cell cycle progression, gene expression, the quality control of proteostasis and the response to geno- and proteotoxic stress. Prior to… (More)
The proteasome is an ATP-dependent multisubunit self-compartmentalised protease complex. It is the major regulator of intracellular proteins turnover. The majority of proteins degraded by proteasomes are modified by covalent attachment of polyubiquitin chains. Substrates include regulatory proteins, transcription factors, components of signal transduction… (More)
In this issue of Molecular Cell, Tomko et al. (2010) establish that the six distinct ATPase subunits of the eukaryotic proteasome form a heterohexameric ring and resolve how the subunits are arranged within the ring.