The proteasome

Current Opinion in Structural Biology

Volumn 7, Issue 2, 1997, Pages 273-278

  Baumeister, Wolfgang ^a   Lupas, Andrei ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME;

ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; REVIEW;

EID: 0030914038     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80036-X     Document Type: Article

References (52)

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47. Enenkel C, Lehmann H, Kipper J, Guckel R, Hilt W, Wolf DH: PRE3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity. FEBS Lett 1994, 341:193-196.
48. Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995, 268:726-731. The covalent attachment of the specific proteasome inhibitor laclacystin to the N-terminal threonine of a subset of eukaryotic β-type subunits provides evidence for the catalytic role of this residue.
49. Seemüller E, Lupas A, Baumeister W: Autocatalytic processing of the 20S proteasome. Nature 1996, 382:468-470. Mutational studies are used to demonstrate that the removal of the prosequences and thus activation of the β-type subunits proceeds by an autocatalytic mechanism and is coupled to proteasome assembly.
50. Chen P, Hochstrasser M: Autocatalytic subunit processing couples active-site formation in the 20S proteasome to completion of assembly. Cell 1996, 86:961-972. This paper provides evidence that β-subunit processing is also autocatalytic in eukaryotes. Beyond preventing premature activation, prosequences may have a critical role in the assembly of the complex, which is not observed in Thermoplasma.
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