Identification and Characterization of a Mammalian Protein Interacting with 20S Proteasome Precursors

The assembly of individual mammalian proteasome subunits into catalytically active 20S proteasome is not well understood. Herein, we report the identification and characterization of human and mouse homologues of the yeast proteasome maturating factor Ump1p. We delineate the region of hUMP1 implicat...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2000-09, Vol.97 (19), p.10348-10353
Main Authors: Burri, Lena, Hockendorff, Jorg, Boehm, Ulrich, Klamp, Thorsten, Dohmen, R. Jurgen, Levy, Frederic
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Antibodies
Biochemistry
Biological Sciences
Blotting, Northern
Cell lines
Cloning, Molecular
Complementary DNA
Cysteine Endopeptidases - metabolism
Humans
Immunoprecipitation
Mice
Mice, Inbred C57BL
Molecular Chaperones - chemistry
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Molecular Sequence Data
Monoclonal antibodies
Multienzyme Complexes - metabolism
Plasmids
Proteasome Endopeptidase Complex
Protein Binding
Protein precursors
Proteins
RNA, Messenger - genetics
Rodents
Saccharomyces cerevisiae - genetics
Sequence Homology, Amino Acid
Yeast
Yeasts
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Summary:The assembly of individual mammalian proteasome subunits into catalytically active 20S proteasome is not well understood. Herein, we report the identification and characterization of human and mouse homologues of the yeast proteasome maturating factor Ump1p. We delineate the region of hUMP1 implicated in the specific interaction with proteasome precursors and show that hUMP1 protein is absent from the mature form of the 20S proteasome. We also show that the transcript level of mammalian UMP1 is increased after IFN-γ treatment and that mammalian UMP1 is functionally related to but not interchangeable with its yeast homologue.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.190268597