1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. Th...

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Detalles Bibliográficos
Autores principales: Singh, Chingakham R., Lovell, Scott, Mehzabeen, Nurjahan, Chowdhury, Wasimul Q., Geanes, Eric S., Battaile, Kevin P., Roelofs, Jeroen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976055/
https://www.ncbi.nlm.nih.gov/pubmed/24699731
http://dx.doi.org/10.1107/S2053230X14003884
Descripción
Sumario:The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.

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