Effects of nucleotides on assembly of the 26S proteasome and degradation of ubiquitin conjugates |
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Authors: | Hoffman Laura Rechsteiner Martin |
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Institution: | (1) Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA |
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Abstract: | We have investigated three aspects of nucleotide usage by the 26S proteasome and its regulatory complex (RC). Both particles hydrolyze the four major ribonucleotides, but ATP and CTP have substantially lower K
_s for hydrolysis than do GTP and UTP. The K
_ for ATP hydrolysis is 15 m for the 26S proteasome and 30 m for the regulatory complex. Formation of the 26S proteasome from the RC and the 20S proteasome requires about 5 m ATP. Although measurable degradation of Ubiquitin(Ub)-lysozyme conjugates occurs in the presence of CTP, GTP, and UTP, the best nucleotide for Ub-conjugate degradation by the 26S proteasome is ATP, with an estimated K
_ of 12 m. In summary, our studies show that micromolar concentrations of ATP are sufficient for several 26S proteasome activities. |
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Keywords: | 26S proteasome regulatory complex nucleotide hydrolysis ubiquitin-conjugate degradation |
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