The 20S proteasome as an assembly platform for the 19S regulatory complex

Klaus Aksel Bjørner Hendil; Franziska Kriegenburg; Keiji Tanaka; Shigeo Murata; Anne-Marie B Lauridsen; Anders H Johnsen; Rasmus Hartmann-Petersen

doi:10.1016/j.jmb.2009.09.038

The 20S proteasome as an assembly platform for the 19S regulatory complex

Klaus Aksel Bjørner Hendil, Franziska Kriegenburg, Keiji Tanaka, Shigeo Murata, Anne-Marie B Lauridsen, Anders H Johnsen, Rasmus Hartmann-Petersen

Biomolecular Sciences

40 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Journal of Molecular Biology
Volume	394
Issue number	2
Pages (from-to)	320-328
Number of pages	9
ISSN	0022-2836
DOIs	https://doi.org/10.1016/j.jmb.2009.09.038
Publication status	Published - 2009

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title = "The 20S proteasome as an assembly platform for the 19S regulatory complex",

abstract = "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.",

author = "Hendil, {Klaus Aksel Bj{\o}rner} and Franziska Kriegenburg and Keiji Tanaka and Shigeo Murata and Lauridsen, {Anne-Marie B} and Johnsen, {Anders H} and Rasmus Hartmann-Petersen",

note = "Keywords: ubiquitin; proteasome; protein assembly; degradation; AAA",

year = "2009",

doi = "10.1016/j.jmb.2009.09.038",

language = "English",

volume = "394",

pages = "320--328",

journal = "Journal of Molecular Biology",

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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 -

The 20S proteasome as an assembly platform for the 19S regulatory complex

Abstract

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