Abstract
Modification of specific intracellular proteins by ubiquitin targets them for degradation. We describe a yeast enzyme, Doa4, that is integral to the degradation of ubiquitinated proteins and is required in diverse physiological processes. Doa4 appears to function late in the proteolytic pathway by cleaving ubiquitin from substrate remnants still bound to protease. The human tre-2 oncogene encodes a deubiquitinating enzyme similar to Doa4, indicating a role for the ubiquitin system in mammalian growth control.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Endopeptidases*
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Endosomal Sorting Complexes Required for Transport
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Fungal Proteins / genetics*
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Fungal Proteins / metabolism
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Genes, Fungal*
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Humans
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Mice
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Mice, Nude
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Molecular Sequence Data
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Mutation
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Oncogene Proteins*
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Oncogene Proteins, Fusion / genetics
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Oncogenes*
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Open Reading Frames
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Phenotype
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Proto-Oncogene Proteins
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Ubiquitin Thiolesterase
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Ubiquitins / metabolism*
Substances
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DOA4 protein, S cerevisiae
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Endosomal Sorting Complexes Required for Transport
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Fungal Proteins
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Oncogene Proteins
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Oncogene Proteins, Fusion
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Proto-Oncogene Proteins
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Ubiquitins
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Endopeptidases
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USP6 protein, human
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Ubiquitin Thiolesterase
Associated data
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GENBANK/L03387
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GENBANK/L08070
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GENBANK/M80041
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GENBANK/T04867
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GENBANK/T09031
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GENBANK/U02518
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GENBANK/Z12710
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GENBANK/Z14720
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GENBANK/Z14811
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GENBANK/Z15701
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GENBANK/Z17750
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GENBANK/Z21167
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GENBANK/Z25610