Abstract
The ability to destroy a particular protein at a particular time is central to the regulation of many cellular processes. Selective proteolysis in eukaryotic cells is carried out primarily by the ubiquitin-proteasome pathway. Attachment of a ubiquitin polymer to an unwanted protein causes it to be degraded by the proteasome. Several classes of enzyme, known as E1s, E2s and E3s, control the stepwise formation of a ubiquitin-protein conjugate. The specificity of substrate selection lies with the E2s and E3s. Here we describe the cloning of a Drosophila E2 gene, UbcD4, which is only expressed in embryos. Its expression pattern in stage 10-11 embryos suggests a role in germ cell development. UbcD4 can interact with the polyubiquitin-binding subunit of the proteasome.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cloning, Molecular
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Cysteine Endopeptidases / metabolism
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Drosophila Proteins*
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Drosophila melanogaster / embryology
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Drosophila melanogaster / enzymology
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Drosophila melanogaster / genetics*
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Embryo, Nonmammalian / cytology
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Embryo, Nonmammalian / enzymology
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Gene Expression Regulation, Developmental
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Gene Expression Regulation, Enzymologic
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In Situ Hybridization
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Ligases / genetics*
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Molecular Sequence Data
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Multienzyme Complexes / metabolism
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Proteasome Endopeptidase Complex
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Protein Binding
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Protein Subunits
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Sequence Homology, Amino Acid
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Ubiquitin-Conjugating Enzymes*
Substances
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Drosophila Proteins
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Multienzyme Complexes
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Protein Subunits
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Ubc4 protein, Drosophila
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Ubiquitin-Conjugating Enzymes
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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Ligases