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Localization of the regulatory particle subunit Semi in the 26S proteasome

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77778

Bohn,  Stefan
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78599

Sakata,  Eri
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77726

Beck,  Florian
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78488

Pathare,  Ganesh Ramnath
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78655

Schnitger,  Jérôme
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78439

Nagy,  Istvan
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77721

Baumeister,  Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77965

Förster,  Friedrich
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Bohn, S., Sakata, E., Beck, F., Pathare, G. R., Schnitger, J., Nagy, I., et al. (2013). Localization of the regulatory particle subunit Semi in the 26S proteasome. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 435(2), 250-254. doi:10.1016/j.bbrc.2013.04.069.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-4553-9
Zusammenfassung
The ubiquitin-proteasome system is responsible for regulated protein degradation in the cell with the 26S proteasome acting as its executive arm. The molecular architecture of this 2.5 MDa complex has been established recently, with the notable exception of the small acidic subunit Semi. Here, we localize the C-terminal helix of Semi binding to the PCI domain of the subunit Rpn7 using cryo-electron microscopy single particle reconstruction of proteasomes purified from yeast cells with semi deletion. The approximate position of the N-terminal region of Semi bridging the cleft between Rpn7 and Rpn3 was inferred based on site-specific cross-linking data of the 26S proteasome. Our structural studies indicate that Semi can assume different conformations in different contexts, which supports the idea that Semi functions as a molecular glue stabilizing the Rpn3/Rpn7 heterodimer. (C) 2013 Elsevier Inc. All rights reserved.