The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes

D M Zaiss; Sybille Standera; H Holzhütter; P.M. Kloetzel; A J Sijts

The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes

D M Zaiss, Sybille Standera, H Holzhütter, P.M. Kloetzel, A J Sijts

Institute of Biochemistry/Charité, Monbijou Strasse 2, D-10117, Berlin, Germany.

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

PI31 is a previously described inhibitor of 20S proteasomes. Using recombinant PI31 we have analyzed its effect on proteasomal hydrolyzing activity of short fluorogenic substrates and of a synthetic 40-mer polypeptide. In addition, we investigated its influence on the activation of 20S proteasome by the proteasome activator PA28. PI31 inhibits polypeptide degradation already at concentrations which only partially inhibit fluorogenic substrate turnover and immunosubunits do not influence the PI31 binding affinity. Furthermore our data demonstrate that PI31 is a potent competitor of PA28-mediated activation.

Original language	English
Pages (from-to)	333-8
Number of pages	6
Journal	FEBS Letters
Volume	457
Issue number	3
Publication status	Published - 3 Sept 1999

Keywords

Amino Acid Sequence
Animals
Autoantigens
Binding, Competitive
Cell Line
Cloning, Molecular
Cysteine Endopeptidases
Cysteine Proteinase Inhibitors
Enzyme Activation
Glutathione Transferase
Humans
Interferon-gamma
Mice
Molecular Sequence Data
Multienzyme Complexes
Muscle Proteins
Proteasome Endopeptidase Complex
Proteins
Recombinant Fusion Proteins
Sequence Homology, Amino Acid
Journal Article
Research Support, Non-U.S. Gov't

Cite this

@article{683a8a8e06ef4551bac586f8fd4c4c70,

title = "The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes",

abstract = "PI31 is a previously described inhibitor of 20S proteasomes. Using recombinant PI31 we have analyzed its effect on proteasomal hydrolyzing activity of short fluorogenic substrates and of a synthetic 40-mer polypeptide. In addition, we investigated its influence on the activation of 20S proteasome by the proteasome activator PA28. PI31 inhibits polypeptide degradation already at concentrations which only partially inhibit fluorogenic substrate turnover and immunosubunits do not influence the PI31 binding affinity. Furthermore our data demonstrate that PI31 is a potent competitor of PA28-mediated activation.",

keywords = "Amino Acid Sequence, Animals, Autoantigens, Binding, Competitive, Cell Line, Cloning, Molecular, Cysteine Endopeptidases, Cysteine Proteinase Inhibitors, Enzyme Activation, Glutathione Transferase, Humans, Interferon-gamma, Mice, Molecular Sequence Data, Multienzyme Complexes, Muscle Proteins, Proteasome Endopeptidase Complex, Proteins, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Journal Article, Research Support, Non-U.S. Gov't",

author = "Zaiss, {D M} and Sybille Standera and H Holzh{\"u}tter and P.M. Kloetzel and Sijts, {A J}",

year = "1999",

month = sep,

day = "3",

language = "English",

volume = "457",

pages = "333--8",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley-Blackwell",

number = "3",

}

TY - JOUR

T1 - The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes

AU - Zaiss, D M

AU - Standera, Sybille

AU - Holzhütter, H

AU - Kloetzel, P.M.

AU - Sijts, A J

PY - 1999/9/3

Y1 - 1999/9/3

N2 - PI31 is a previously described inhibitor of 20S proteasomes. Using recombinant PI31 we have analyzed its effect on proteasomal hydrolyzing activity of short fluorogenic substrates and of a synthetic 40-mer polypeptide. In addition, we investigated its influence on the activation of 20S proteasome by the proteasome activator PA28. PI31 inhibits polypeptide degradation already at concentrations which only partially inhibit fluorogenic substrate turnover and immunosubunits do not influence the PI31 binding affinity. Furthermore our data demonstrate that PI31 is a potent competitor of PA28-mediated activation.

AB - PI31 is a previously described inhibitor of 20S proteasomes. Using recombinant PI31 we have analyzed its effect on proteasomal hydrolyzing activity of short fluorogenic substrates and of a synthetic 40-mer polypeptide. In addition, we investigated its influence on the activation of 20S proteasome by the proteasome activator PA28. PI31 inhibits polypeptide degradation already at concentrations which only partially inhibit fluorogenic substrate turnover and immunosubunits do not influence the PI31 binding affinity. Furthermore our data demonstrate that PI31 is a potent competitor of PA28-mediated activation.

KW - Amino Acid Sequence

KW - Animals

KW - Autoantigens

KW - Binding, Competitive

KW - Cell Line

KW - Cloning, Molecular

KW - Cysteine Endopeptidases

KW - Cysteine Proteinase Inhibitors

KW - Enzyme Activation

KW - Glutathione Transferase

KW - Humans

KW - Interferon-gamma

KW - Mice

KW - Molecular Sequence Data

KW - Multienzyme Complexes

KW - Muscle Proteins

KW - Proteasome Endopeptidase Complex

KW - Proteins

KW - Recombinant Fusion Proteins

KW - Sequence Homology, Amino Acid

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - Article

C2 - 10471803

SN - 0014-5793

VL - 457

SP - 333

EP - 338

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes

Abstract

Keywords

Fingerprint

Cite this