Structure and structure formation of the 20S proteasome

Marion Schmidt, Gunter Schmidtke, Peter M. Kloetzel

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Eukaryotic 20S proteasomes are complex oligomeric proteins. The maturation process of the 14 different α- and β-subunits has to occur in a highly coordinate manner. In addition β-subunits are synthesized as proproteins and correct processing has to be guaranteed during complex maturation. The structure formation can be subdivided in different phases. The knowledge of the individual phases is summarized in this publication. As a first step the newly synthesized monomers have to adopt the correct tertiary structure, a process that might be supported in the case of the β-subunits by the intramolecular chaperone activity postulated for the prosequences. Subsequently the α-subunits form ring-like structures thereby providing docking sites for the different β-subunits. The result most likely is a double ring structure (13S precursor) representing half-proteasomes, which contain immature proproteins. Two 13S precursors associate to form the proteolytically inactive 16S assembly intermediate which still contains unprocessed β-monomers. In addition the chaperone Hsc73 is present within these particles suggesting an essential role during the structure formation process. The processing of monomers with an N-terminal threonine occurs within the 16S particles and is achieved autocatalytically by two subsequent processing events finally leading to the mature, active 20S proteasome.

Original languageEnglish (US)
Pages (from-to)103-112
Number of pages10
JournalMolecular Biology Reports
Volume24
Issue number1-2
StatePublished - Mar 1997
Externally publishedYes

Fingerprint

Proteasome Endopeptidase Complex
Monomers
Processing
Threonine
Proteins

Keywords

  • Assembly mechanism
  • Autocatalytic activation
  • Circular assemblies
  • Proprotein processing
  • Proteasome
  • Proteasome maturation

ASJC Scopus subject areas

  • Genetics
  • Cell Biology
  • Biochemistry

Cite this

Schmidt, M., Schmidtke, G., & Kloetzel, P. M. (1997). Structure and structure formation of the 20S proteasome. Molecular Biology Reports, 24(1-2), 103-112.

Structure and structure formation of the 20S proteasome. / Schmidt, Marion; Schmidtke, Gunter; Kloetzel, Peter M.

In: Molecular Biology Reports, Vol. 24, No. 1-2, 03.1997, p. 103-112.

Research output: Contribution to journalArticle

Schmidt, M, Schmidtke, G & Kloetzel, PM 1997, 'Structure and structure formation of the 20S proteasome', Molecular Biology Reports, vol. 24, no. 1-2, pp. 103-112.
Schmidt M, Schmidtke G, Kloetzel PM. Structure and structure formation of the 20S proteasome. Molecular Biology Reports. 1997 Mar;24(1-2):103-112.
Schmidt, Marion ; Schmidtke, Gunter ; Kloetzel, Peter M. / Structure and structure formation of the 20S proteasome. In: Molecular Biology Reports. 1997 ; Vol. 24, No. 1-2. pp. 103-112.
@article{215c7af18cdc450e86dd69b3c1208078,
title = "Structure and structure formation of the 20S proteasome",
abstract = "Eukaryotic 20S proteasomes are complex oligomeric proteins. The maturation process of the 14 different α- and β-subunits has to occur in a highly coordinate manner. In addition β-subunits are synthesized as proproteins and correct processing has to be guaranteed during complex maturation. The structure formation can be subdivided in different phases. The knowledge of the individual phases is summarized in this publication. As a first step the newly synthesized monomers have to adopt the correct tertiary structure, a process that might be supported in the case of the β-subunits by the intramolecular chaperone activity postulated for the prosequences. Subsequently the α-subunits form ring-like structures thereby providing docking sites for the different β-subunits. The result most likely is a double ring structure (13S precursor) representing half-proteasomes, which contain immature proproteins. Two 13S precursors associate to form the proteolytically inactive 16S assembly intermediate which still contains unprocessed β-monomers. In addition the chaperone Hsc73 is present within these particles suggesting an essential role during the structure formation process. The processing of monomers with an N-terminal threonine occurs within the 16S particles and is achieved autocatalytically by two subsequent processing events finally leading to the mature, active 20S proteasome.",
keywords = "Assembly mechanism, Autocatalytic activation, Circular assemblies, Proprotein processing, Proteasome, Proteasome maturation",
author = "Marion Schmidt and Gunter Schmidtke and Kloetzel, {Peter M.}",
year = "1997",
month = "3",
language = "English (US)",
volume = "24",
pages = "103--112",
journal = "Molecular Biology Reports",
issn = "0301-4851",
publisher = "Springer Netherlands",
number = "1-2",

}

TY - JOUR

T1 - Structure and structure formation of the 20S proteasome

AU - Schmidt, Marion

AU - Schmidtke, Gunter

AU - Kloetzel, Peter M.

PY - 1997/3

Y1 - 1997/3

N2 - Eukaryotic 20S proteasomes are complex oligomeric proteins. The maturation process of the 14 different α- and β-subunits has to occur in a highly coordinate manner. In addition β-subunits are synthesized as proproteins and correct processing has to be guaranteed during complex maturation. The structure formation can be subdivided in different phases. The knowledge of the individual phases is summarized in this publication. As a first step the newly synthesized monomers have to adopt the correct tertiary structure, a process that might be supported in the case of the β-subunits by the intramolecular chaperone activity postulated for the prosequences. Subsequently the α-subunits form ring-like structures thereby providing docking sites for the different β-subunits. The result most likely is a double ring structure (13S precursor) representing half-proteasomes, which contain immature proproteins. Two 13S precursors associate to form the proteolytically inactive 16S assembly intermediate which still contains unprocessed β-monomers. In addition the chaperone Hsc73 is present within these particles suggesting an essential role during the structure formation process. The processing of monomers with an N-terminal threonine occurs within the 16S particles and is achieved autocatalytically by two subsequent processing events finally leading to the mature, active 20S proteasome.

AB - Eukaryotic 20S proteasomes are complex oligomeric proteins. The maturation process of the 14 different α- and β-subunits has to occur in a highly coordinate manner. In addition β-subunits are synthesized as proproteins and correct processing has to be guaranteed during complex maturation. The structure formation can be subdivided in different phases. The knowledge of the individual phases is summarized in this publication. As a first step the newly synthesized monomers have to adopt the correct tertiary structure, a process that might be supported in the case of the β-subunits by the intramolecular chaperone activity postulated for the prosequences. Subsequently the α-subunits form ring-like structures thereby providing docking sites for the different β-subunits. The result most likely is a double ring structure (13S precursor) representing half-proteasomes, which contain immature proproteins. Two 13S precursors associate to form the proteolytically inactive 16S assembly intermediate which still contains unprocessed β-monomers. In addition the chaperone Hsc73 is present within these particles suggesting an essential role during the structure formation process. The processing of monomers with an N-terminal threonine occurs within the 16S particles and is achieved autocatalytically by two subsequent processing events finally leading to the mature, active 20S proteasome.

KW - Assembly mechanism

KW - Autocatalytic activation

KW - Circular assemblies

KW - Proprotein processing

KW - Proteasome

KW - Proteasome maturation

UR - http://www.scopus.com/inward/record.url?scp=0031105201&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031105201&partnerID=8YFLogxK

M3 - Article

C2 - 9228290

AN - SCOPUS:0031105201

VL - 24

SP - 103

EP - 112

JO - Molecular Biology Reports

JF - Molecular Biology Reports

SN - 0301-4851

IS - 1-2

ER -