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J Biol Chem, Vol. 274, Issue 31, 21943-21952, July 30, 1999
From the Departments of Internal Medicine and Biochemistry,
Biochemistry and Molecular Biology Graduate Program, University of
Texas-Southwestern Medical Center, Dallas, Texas 75235-8573
The 26 S proteasome of eukaryotes is responsible
for the degradation of proteins targeted for proteolysis by the
ubiquitin system. Yeast has been an important model organism for
understanding eukaryotic proteasome structure and function. Toward a
quantitative characterization of the proteasome, we have determined the
localization, cellular levels, and stoichiometry of proteasome
subunits. The subcellular localization of two ATPase components of the
regulatory complex of the proteasome, Sug2/Rpt4 and Sug1/Rpt6, and a
subunit of the 20 S proteasome, Pre1, were determined by
immunofluorescence. In contrast to findings in multicellular organisms,
these proteins are localized almost exclusively to the nucleus
throughout the cell cycle. We have also determined the cellular
abundance and stoichiometry of these proteasome subunits. Sug1/Rpt6,
Sug2/Rpt4, and Pre1 are present in roughly equal stoichiometry with an
abundance of 15,000-30,000 molecules/cell, corresponding to a
concentration of 13-26 µM in the nucleus. Also, in
contrast to mammalian cells, we find no evidence of a p27-containing
"modulator" of the proteasome in yeast. This information will be
useful in comparing and contrasting the yeast and mammalian proteasomes
and should contribute to a mechanistic understanding of how this
complex functions.
Subcellular Localization, Stoichiometry, and Protein Levels
of 26 S Proteasome Subunits in Yeast
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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