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	Biochem. Biophys. Res. Commun. Aug (2007); 359(3):503-9
Structural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasome-
Nakamura Y, Umehara T, Tanaka A, Horikoshi M, Padmanabhan B, Yokoyama S
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan-
Abstract: The 26S proteasome-dependent protein degradation is an evolutionarily conserved process- The mammalian oncoprotein gankyrin, which associates with S6 of the proteasome, facilitates the degradation of pRb, and thus possibly acts as a bridging factor between the proteasome and its substrates- However, the mechanism of the proteasome-dependent protein degradation in yeast is poorly understood- Here, we report the tertiary structure of the complex between Nas6 and a C-terminal domain of Rpt3, which are the yeast orthologues of gankyrin and S6, respectively- The concave region of Nas6 bound to the alpha-helical domain of Rpt3- The stable interaction between Nas6 and Rpt3 was mediated by intermolecular interactions composed of complementary charged patches- The recognition of Rpt3 by Nas6 in the crystal suggests that Nas6 is indeed a subunit of the 26S proteasome- These results provide a structural basis for the association between Nas6 and the heterohexameric ATPase ring of the proteasome through Rpt3-
[PUBMED: 17555716]