Abstract
Ubiquitinated proteins are degraded by a 26 S ATP-dependent protease. SDS-polyacrylamide gel electrophoresis analysis of the purified 26 S enzyme reveals more than 20 polypeptides ranging in apparent molecular masses from 20 to 110 kDa. Although many of the subunits smaller than 30 kDa are members of the multicatalytic protease family, the identity and function of the larger polypeptides have remained unknown. We report here the cDNA sequence for subunit 4, a 51-kDa chain of the 26 S protease. Subunit 4 belongs to a recently identified eukaryotic ATPase family, which includes proteins involved in peroxisome formation, secretion, and human immunodeficiency virus gene expression. Subunit 4 also shows weak similarity to ClpA, the ATP-binding subunit of the Escherichia coli protease, Clp.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / genetics*
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Amino Acid Sequence
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Animals
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Base Sequence
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Cloning, Molecular
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DNA / genetics
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DNA / isolation & purification
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Escherichia coli / genetics
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HeLa Cells
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Humans
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Macromolecular Substances
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Molecular Sequence Data
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Oligodeoxyribonucleotides
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Oligonucleotides, Antisense
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Peptide Hydrolases / blood
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Peptide Hydrolases / genetics*
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Peptide Hydrolases / isolation & purification
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Proteasome Endopeptidase Complex*
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Protein Biosynthesis
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Sequence Homology, Amino Acid
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Transcription, Genetic
Substances
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Macromolecular Substances
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Oligodeoxyribonucleotides
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Oligonucleotides, Antisense
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DNA
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Peptide Hydrolases
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Proteasome Endopeptidase Complex
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ATP dependent 26S protease
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Adenosine Triphosphatases
Associated data
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GENBANK/D12746
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GENBANK/D12747
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GENBANK/D12748
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GENBANK/D12749
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GENBANK/D12750
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GENBANK/D12751
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GENBANK/D12752
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GENBANK/D12753
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GENBANK/L02426
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GENBANK/M98479