PMID- 10419517
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 31
DP  - 1999 Jul 30
TI  - Subcellular localization, stoichiometry, and protein levels of 26 S proteasome
      subunits in yeast.
PG  - 21943-52
AB  - 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 microM 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.
FAU - Russell, S J
AU  - Russell SJ
AD  - Departments of Internal Medicine and Biochemistry, Biochemistry and Molecular
      Biology Graduate Program, University of Texas-Southwestern Medical Center,
      Dallas, Texas 75235-8573, USA.
FAU - Steger, K A
AU  - Steger KA
FAU - Johnston, S A
AU  - Johnston SA
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Epitopes)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.4.- (Peptide Hydrolases)
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
RN  - EC 3.4.99.- (ATP dependent 26S protease)
SB  - IM
MH  - Amino Acid Sequence
MH  - Blotting, Western
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Epitopes/analysis
MH  - Humans
MH  - Kinetics
MH  - Macromolecular Substances
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Peptide Hydrolases/chemistry/genetics/*metabolism
MH  - Polymerase Chain Reaction
MH  - *Proteasome Endopeptidase Complex
MH  - Protein Biosynthesis
MH  - Recombinant Proteins/chemistry/isolation & purification/metabolism
MH  - Saccharomyces cerevisiae/*enzymology/genetics
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
EDAT- 1999/07/27 00:00
MHDA- 1999/07/27 00:01
CRDT- 1999/07/27 00:00
PHST- 1999/07/27 00:00 [pubmed]
PHST- 1999/07/27 00:01 [medline]
PHST- 1999/07/27 00:00 [entrez]
AID - 10.1074/jbc.274.31.21943 [doi]
AID - S0021-9258(19)72470-3 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 30;274(31):21943-52. doi: 10.1074/jbc.274.31.21943.