A proteasome howdunit: the case of the missing signal

Article Abstract:

The question of whether or not ODC and p21(super.cip1) make up a class of proteins that can be degraded by the proteasome in vivo without ubiquitination to help is discussed in this minireview article. Reasons for eukaryotic proteasomes to have evolved such strong preference for ubiquitinated substrates are presented, given that they differ in this respect from the very similar prokaryotic counterparts.

Physiological aspects, Prokaryotes, Proteins, Cellular signal transduction, Proteolysis, Ubiquitin

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Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system

Article Abstract:

Ubiquitin-proteasome system (UPS) possibly consists of the recruitment of ubiquitinated proteins to the 26S proteasome. An additional layer of substrate selectivity in UPS may be provided by the recruitment of substrates to the proteasome by the multiubiquitin chain binding proteins (MCBPs).

Analysis, Protein binding, Ubiquitin-proteasome system

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The exosome: a proteasome for RNA?

Article Abstract:

Organization and functions of the exosome are discussed in this review article. In yeast it is a protein complex made up of a core of at least ten proteins, all ten proposed to be active 3'-to-5' exoribonucleases, and is found in the nucleus and cytoplasm. It has an important RNA processing/degradation function in eukaryotic cells and probably has functions not yet known. Evidence indicates that it is conserved in eukaryotes. Differences in structure may exist from species to species.

Statistical Data Included, RNA, Yeast, Yeast (Food product), Exonucleases

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