Regulatory proteins of the proteasome

G. N. DeMartino, Clive A. Slaughter

Research output: Contribution to journalReview article

42 Citations (Scopus)

Abstract

The function of the proteasome is controlled by a variety of specific regulatory proteins including activators, inhibitors, and modulators. Two recently discovered activators, termed PA28 and PA700, bind to the terminal rings of the proteasome to form proteasome-regulator complexes which display greatly increased proteolytic activity. PA28 is a high-affinity activator of the proteasome's multiple peptidase activities. The carboxyl terminus of PA28 is required for its binding to the proteasome. PA700 binds to the proteasome via an ATP-dependent mechanism. PA700 has ATPase activity, and at least four of PA700's 16 subunits are members of a protein family containing a concensus sequence for ATP binding. Proteasome-PA700 complexes are activated with respect to both the hydrolysis of peptide substrates and the hydrolysis of ubiquitinated proteins.

Original languageEnglish (US)
Pages (from-to)314-324
Number of pages11
JournalEnzyme and Protein
Volume47
Issue number4-6
StatePublished - Dec 1 1993
Externally publishedYes

Fingerprint

Proteasome Endopeptidase Complex
Proteins
Hydrolysis
Adenosine Triphosphate
Ubiquitinated Proteins
Modulators
Adenosine Triphosphatases
Peptide Hydrolases
Peptides
Substrates

Keywords

  • Activators
  • ATPase
  • PA28
  • PA700
  • Proteasome
  • Regulators

ASJC Scopus subject areas

  • Biochemistry

Cite this

Regulatory proteins of the proteasome. / DeMartino, G. N.; Slaughter, Clive A.

In: Enzyme and Protein, Vol. 47, No. 4-6, 01.12.1993, p. 314-324.

Research output: Contribution to journalReview article

DeMartino, GN & Slaughter, CA 1993, 'Regulatory proteins of the proteasome', Enzyme and Protein, vol. 47, no. 4-6, pp. 314-324.
DeMartino, G. N. ; Slaughter, Clive A. / Regulatory proteins of the proteasome. In: Enzyme and Protein. 1993 ; Vol. 47, No. 4-6. pp. 314-324.
@article{f6317e03964846ea8ed52ddab6541442,
title = "Regulatory proteins of the proteasome",
abstract = "The function of the proteasome is controlled by a variety of specific regulatory proteins including activators, inhibitors, and modulators. Two recently discovered activators, termed PA28 and PA700, bind to the terminal rings of the proteasome to form proteasome-regulator complexes which display greatly increased proteolytic activity. PA28 is a high-affinity activator of the proteasome's multiple peptidase activities. The carboxyl terminus of PA28 is required for its binding to the proteasome. PA700 binds to the proteasome via an ATP-dependent mechanism. PA700 has ATPase activity, and at least four of PA700's 16 subunits are members of a protein family containing a concensus sequence for ATP binding. Proteasome-PA700 complexes are activated with respect to both the hydrolysis of peptide substrates and the hydrolysis of ubiquitinated proteins.",
keywords = "Activators, ATPase, PA28, PA700, Proteasome, Regulators",
author = "DeMartino, {G. N.} and Slaughter, {Clive A.}",
year = "1993",
month = "12",
day = "1",
language = "English (US)",
volume = "47",
pages = "314--324",
journal = "Enzyme and Protein",
issn = "1019-6773",
publisher = "S. Karger AG",
number = "4-6",

}

TY - JOUR

T1 - Regulatory proteins of the proteasome

AU - DeMartino, G. N.

AU - Slaughter, Clive A.

PY - 1993/12/1

Y1 - 1993/12/1

N2 - The function of the proteasome is controlled by a variety of specific regulatory proteins including activators, inhibitors, and modulators. Two recently discovered activators, termed PA28 and PA700, bind to the terminal rings of the proteasome to form proteasome-regulator complexes which display greatly increased proteolytic activity. PA28 is a high-affinity activator of the proteasome's multiple peptidase activities. The carboxyl terminus of PA28 is required for its binding to the proteasome. PA700 binds to the proteasome via an ATP-dependent mechanism. PA700 has ATPase activity, and at least four of PA700's 16 subunits are members of a protein family containing a concensus sequence for ATP binding. Proteasome-PA700 complexes are activated with respect to both the hydrolysis of peptide substrates and the hydrolysis of ubiquitinated proteins.

AB - The function of the proteasome is controlled by a variety of specific regulatory proteins including activators, inhibitors, and modulators. Two recently discovered activators, termed PA28 and PA700, bind to the terminal rings of the proteasome to form proteasome-regulator complexes which display greatly increased proteolytic activity. PA28 is a high-affinity activator of the proteasome's multiple peptidase activities. The carboxyl terminus of PA28 is required for its binding to the proteasome. PA700 binds to the proteasome via an ATP-dependent mechanism. PA700 has ATPase activity, and at least four of PA700's 16 subunits are members of a protein family containing a concensus sequence for ATP binding. Proteasome-PA700 complexes are activated with respect to both the hydrolysis of peptide substrates and the hydrolysis of ubiquitinated proteins.

KW - Activators

KW - ATPase

KW - PA28

KW - PA700

KW - Proteasome

KW - Regulators

UR - http://www.scopus.com/inward/record.url?scp=0027707471&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027707471&partnerID=8YFLogxK

M3 - Review article

VL - 47

SP - 314

EP - 324

JO - Enzyme and Protein

JF - Enzyme and Protein

SN - 1019-6773

IS - 4-6

ER -