TY - JOUR
T1 - The 20S proteasome as an assembly platform for the 19S regulatory complex
AU - Hendil, Klaus Aksel Bjørner
AU - Kriegenburg, Franziska
AU - Tanaka, Keiji
AU - Murata, Shigeo
AU - Lauridsen, Anne-Marie B
AU - Johnsen, Anders H
AU - Hartmann-Petersen, Rasmus
N1 - Keywords: ubiquitin; proteasome; protein assembly; degradation; AAA
PY - 2009
Y1 - 2009
N2 - 26S proteasomes consist of cylindrical 20S proteasomes with 19S regulatory complexes attached to the ends. Treatment with high concentrations of salt causes the regulatory complexes to separate into two sub-complexes, the base, which is in contact with the 20S proteasome, and the lid, which is the distal part of the 19S complex. Here, we describe two assembly intermediates of the human regulatory complex. One is a dimer of the two ATPase subunits, Rpt3 and Rpt6. The other is a complex of nascent Rpn2, Rpn10, Rpn11, Rpn13, and Txnl1, attached to preexisting 20S proteasomes. This early assembly complex does not yet contain Rpn1 or any of the ATPase subunits of the base. Thus, assembly of 19S regulatory complexes takes place on preexisting 20S proteasomes, and part of the lid is assembled before the base.
AB - 26S proteasomes consist of cylindrical 20S proteasomes with 19S regulatory complexes attached to the ends. Treatment with high concentrations of salt causes the regulatory complexes to separate into two sub-complexes, the base, which is in contact with the 20S proteasome, and the lid, which is the distal part of the 19S complex. Here, we describe two assembly intermediates of the human regulatory complex. One is a dimer of the two ATPase subunits, Rpt3 and Rpt6. The other is a complex of nascent Rpn2, Rpn10, Rpn11, Rpn13, and Txnl1, attached to preexisting 20S proteasomes. This early assembly complex does not yet contain Rpn1 or any of the ATPase subunits of the base. Thus, assembly of 19S regulatory complexes takes place on preexisting 20S proteasomes, and part of the lid is assembled before the base.
U2 - 10.1016/j.jmb.2009.09.038
DO - 10.1016/j.jmb.2009.09.038
M3 - Journal article
C2 - 19781552
SN - 0022-2836
VL - 394
SP - 320
EP - 328
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 2
ER -