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EMBO Rep. 2003 Oct;4(10):959-63. Epub 2003 Sep 12.

Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly.

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  • 1Institut für Biochemie, Humboldt Universität zu Berlin, Universitätsklinikum Charité, Monbijoustrasse 2, D-10117 Berlin, Germany.


Proteasomes are multisubunit proteases that are responsible for regulated proteolysis. The degradation of the proteasomal maturation factor, named Ump1 in yeast, completes the autocatalytic processing of inactive precursor complexes into the proteolytically active core particle (CP) of the proteasome. We have identified Blm3, a conserved nuclear protein, as a new component of Ump1-associated precursor complexes. A lack of Blm3 resulted in an increased rate of precursor processing and an accelerated turnover of Ump1, which suggests that Blm3 prevents premature activation of proteasomal CPs. On the basis of biochemical fractionation experiments combined with in vivo localization studies, we propose that Blm3 joins nascent CPs inside the nucleus to coordinate late stages of proteasome assembly in yeast.

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