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2
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Proteasome function is dispensable under normal but not under heat-shock conditions in Thermoplasma acidophilum
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Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R. The 20S proteasome of Streptomyces coelicolor. J Bacteriol. 180:1998;5448-5453.
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Pouch M.-N., Cournoyer B., Baumeister W. Characterization of the 20S proteasome from the actinomycete Frankia. Mol Microbiol. 35:2000;368-377.
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Subunit topology of the Rhodococcus proteasome
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Zühl F., Tamura T., Dolenc I., Cejka Z., Nagy I., De Mot R., Baumeister W. Subunit topology of the Rhodococcus proteasome. FEBS Lett. 400:1997;83-90.
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A comprehensive overview of proteasome research, with the main focus on 26S proteasomes.
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Voges D., Zwickl P., Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem. 68:1999;1015-1068. A comprehensive overview of proteasome research, with the main focus on 26S proteasomes.
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Mutational and biochemical analyses of the specificity of the proteasomal β subunits are presented. All proteolytic activities could be assigned to subunits β1, β2 and β5, excluding the existence of additional active sites.
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Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase 1
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The authors describe the analysis of the cleavage products of enolase degraded by yeast proteasomes. A comparison of the fragments generated by wild-type and mutant proteasomes demonstrated that the product length is not dependent on the number of active sites.
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Nussbaum A.K., Dick T.P., Keilholz W., Schirle M., Stevanovic S., Dietz K., Heinemeyer W., Groll M., Wolf D.H., Huber R.et al. Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase 1. Proc Natl Acad Sci USA. 95:1998;12504-12509. The authors describe the analysis of the cleavage products of enolase degraded by yeast proteasomes. A comparison of the fragments generated by wild-type and mutant proteasomes demonstrated that the product length is not dependent on the number of active sites.
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A cyclical bite-chew mechanism for protein breakdown by proteasomes is proposed, based on the finding of allosteric regulation of active sites.
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Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
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The authors report the discovery of the short-lived chaperone Ump1p, which is required for the correct maturation of the yeast 20S proteasome.
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Dolenc I., Seemüller E., Baumeister W. Decelerated degradation of short peptides by the 20S proteasome. FEBS Lett. 434:1998;357-361.
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Single-particle three-dimensional electron microscopy provided the first insights into the structural organization of the 19S regulatory complex. Image analysis reveals a weak flexible linkage between the regulatory complex and the proteolytic core.
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Walz J., Erdmann A., Kania M., Typke D., Koster A.J., Baumeister W. 26S proteasome structure revealed by three-dimensional electron microscopy. J Struct Biol. 121:1998;19-29. Single-particle three-dimensional electron microscopy provided the first insights into the structural organization of the 19S regulatory complex. Image analysis reveals a weak flexible linkage between the regulatory complex and the proteolytic core.
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A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
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The dissection of the 19S regulator of the yeast 26S proteasome into 'lid' and 'base' subcomplexes using functional and structural analyses. The lid is essential for the degradation of ubiquitinated substrates, whereas the base is responsible for ATP-dependent degradation.
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Glickman M.H., Rubin D.M., Coux O., Wefes I., Pfeifer G., Cjeka Z., Baumeister W., Fried V.A., Finley D. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell. 94:1998;615-623. The dissection of the 19S regulator of the yeast 26S proteasome into 'lid' and 'base' subcomplexes using functional and structural analyses. The lid is essential for the degradation of ubiquitinated substrates, whereas the base is responsible for ATP-dependent degradation.
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Comparison of human COP9 signalosome and 26S proteasome 'lid'
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The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex
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Mutational analysis in yeast revealed that the proteasomal ATPases function in a nonredundant manner.
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Rubin D.M., Glickman M.H., Larsen C.N., Dhruvakumar S., Finley D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17:1998;4909-4919. Mutational analysis in yeast revealed that the proteasomal ATPases function in a nonredundant manner.
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39
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The base of the proteasome regulatory particle exhibits chaperone-like activity
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Surprisingly, the 19S regulator of the 26S proteasome is shown to refold denatured citrate synthase. This chaperone-like activity is mapped to the base subcomplex of the regulator. The refolding of a substrate protein is opposite to the assumed function of the 19S regulator in unfolding substrate proteins.
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Braun B.C., Glickman M., Kraft R., Dahlmann B., Kloetzel P.M., Finley D., Schmidt M. The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat Cell Biol. 1:1999;221-226. Surprisingly, the 19S regulator of the 26S proteasome is shown to refold denatured citrate synthase. This chaperone-like activity is mapped to the base subcomplex of the regulator. The refolding of a substrate protein is opposite to the assumed function of the 19S regulator in unfolding substrate proteins.
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41
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A 220-kDa activator complex of the 26S proteasome in insects and humans - A role in type II programmed insect muscle cell death and cross-activation of proteasomes from different species
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Hastings R.A., Eyheralde I., Dawson S.P., Walker G., Reynolds S.E., Billett M.A., Mayer R.J. A 220-kDa activator complex of the 26S proteasome in insects and humans - a role in type II programmed insect muscle cell death and cross-activation of proteasomes from different species. J Biol Chem. 274:1999;25691-25700.
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