TY - JOUR
T1 - Localization of the regulatory particle subunit Sem1 in the 26S proteasome
AU - Bohn, Stefan
AU - Sakata, Eri
AU - Beck, Florian
AU - Pathare, Ganesh R
AU - Schnitger, Jérôme
AU - Nágy, Istvan
AU - Baumeister, Wolfgang
AU - Förster, Friedrich
N1 - Copyright © 2013 Elsevier Inc. All rights reserved.
PY - 2013
Y1 - 2013
N2 - 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 Sem1. Here, we localize the C-terminal helix of Sem1 binding to the PCI domain of the subunit Rpn7 using cryo-electron microscopy single particle reconstruction of proteasomes purified from yeast cells with sem1 deletion. The approximate position of the N-terminal region of Sem1 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 Sem1 can assume different conformations in different contexts, which supports the idea that Sem1 functions as a molecular glue stabilizing the Rpn3/Rpn7 heterodimer.
AB - 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 Sem1. Here, we localize the C-terminal helix of Sem1 binding to the PCI domain of the subunit Rpn7 using cryo-electron microscopy single particle reconstruction of proteasomes purified from yeast cells with sem1 deletion. The approximate position of the N-terminal region of Sem1 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 Sem1 can assume different conformations in different contexts, which supports the idea that Sem1 functions as a molecular glue stabilizing the Rpn3/Rpn7 heterodimer.
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Proteasome Endopeptidase Complex
KW - Protein Subunits
KW - Regulatory Elements, Transcriptional
KW - Saccharomyces cerevisiae Proteins
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000320828300015&KeyUID=WOS:000320828300015
U2 - 10.1016/j.bbrc.2013.04.069
DO - 10.1016/j.bbrc.2013.04.069
M3 - Article
C2 - 23643786
SN - 0006-291X
VL - 435
SP - 250
EP - 254
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -