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• W1856816861 endingPage "6584" @default.
• W1856816861 startingPage "6575" @default.
• W1856816861 abstract "We have isolated the RPN9 gene by two-hybrid screening with, as bait, RPN10 (formerly SUN1), which encodes a multiubiquitin chain receptor residing in the regulatory particle of the 26S proteasome. Rpn9 is a nonessential subunit of the regulatory particle of the 26S proteasome, but the deletion of this gene results in temperature-sensitive growth. At the restrictive temperature, the Δrpn9 strain accumulated multiubiquitinated proteins, indicating that the RPN9function is needed for the 26S proteasome activity at a higher temperature. We analyzed the proteasome fractions separated by glycerol density gradient centrifugation by native polyacrylamide gel electrophoresis and found that a smaller amount of the 26S proteasome was produced in the Δrpn9 cells and that the 26S proteasome was shifted to lighter fractions than expected. The incomplete proteasome complexes were found to accumulate in the Δrpn9 cells. Furthermore, Rpn10 was not detected in the fractions containing proteasomes of the Δrpn9 cells. These results indicate that Rpn9 is needed for incorporating Rpn10 into the 26S proteasome and that Rpn9 participates in the assembly and/or stability of the 26S proteasome." @default.
• W1856816861 created "2016-06-24" @default.
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• W1856816861 date "1999-10-01" @default.
• W1856816861 modified "2023-10-17" @default.
• W1856816861 title "Rpn9 Is Required for Efficient Assembly of the Yeast 26S Proteasome" @default.
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• W1856816861 doi "https://doi.org/10.1128/mcb.19.10.6575" @default.
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