The 26S-proteasome

Regulation and substrate recognition

Simon Dawson, Richard Hastings, Katsuhiko Takayanagi, Stuart Reynolds, P. Lőw, Michael Billett, R. John Mayer

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

There is extensive reprogramming of the ATPase regulators of the 26S proteasome before the programmed elimination of the abdominal intersegmental muscles (ISM) after eclosion in Manduca sexta [1]. This extensive ATPase reprogramming only occurs in ISM which are destined to die and not in flight muscle (FM). The MS73 ATPase also increases in the proleg retractor muscles which die at a developmentally different stage to ISM. The non-ATPase regulator S5a shows a similar increase to the ATPase regulators. We have cloned the Manduca SUG2 ATPase and shown that this ATPase is a component of the 26S proteasome. This ATPase shows a similar increase in concentration to the other ATPases in 26S proteasomes before muscle death. The SUG2 ATPase is also associated with other smaller complexes besides the 26S proteasome which act as activators of the 26S proteasome. Finally, in a yeast two-hybrid genetic screen we have identified a protein in human brain which interacts with the MS73 ATPase (and human S6). The interacting protein contains 6 ankyrin repeats and is co-immunoprecipitated with anti-MS73 antiserum after in vitro transcription/translation. The ankyrin repeat protein may interact with the MS73 ATPase as part of the substrate recognition process by the 26S proteasome. Many proteins degraded by the 26S proteasome contain ankyrin repeats, e.g. IkB and some cyclins: binding through ankyrin repeats to an ATPase regulator may complement protein ubiquitination and S5a binding as recognition signals by the 26S proteasome.

Original languageEnglish
Pages (from-to)39-44
Number of pages6
JournalMolecular Biology Reports
Volume24
Issue number1-2
Publication statusPublished - Mar 1997

Fingerprint

Adenosine Triphosphatases
Substrates
Ankyrin Repeat
Muscle
Muscles
Manduca
ATP dependent 26S protease
Proteins
S 6
Abdominal Muscles
Cyclins
Ubiquitination
Transcription
Yeast
Immune Sera
Brain
Complement System Proteins
Yeasts

Keywords

  • 26S proteasome
  • ATPase
  • Programmed cell death
  • Regulators

ASJC Scopus subject areas

  • Genetics
  • Cell Biology
  • Biochemistry

Cite this

Dawson, S., Hastings, R., Takayanagi, K., Reynolds, S., Lőw, P., Billett, M., & John Mayer, R. (1997). The 26S-proteasome: Regulation and substrate recognition. Molecular Biology Reports, 24(1-2), 39-44.

The 26S-proteasome : Regulation and substrate recognition. / Dawson, Simon; Hastings, Richard; Takayanagi, Katsuhiko; Reynolds, Stuart; Lőw, P.; Billett, Michael; John Mayer, R.

In: Molecular Biology Reports, Vol. 24, No. 1-2, 03.1997, p. 39-44.

Research output: Contribution to journalArticle

Dawson, S, Hastings, R, Takayanagi, K, Reynolds, S, Lőw, P, Billett, M & John Mayer, R 1997, 'The 26S-proteasome: Regulation and substrate recognition', Molecular Biology Reports, vol. 24, no. 1-2, pp. 39-44.
Dawson S, Hastings R, Takayanagi K, Reynolds S, Lőw P, Billett M et al. The 26S-proteasome: Regulation and substrate recognition. Molecular Biology Reports. 1997 Mar;24(1-2):39-44.
Dawson, Simon ; Hastings, Richard ; Takayanagi, Katsuhiko ; Reynolds, Stuart ; Lőw, P. ; Billett, Michael ; John Mayer, R. / The 26S-proteasome : Regulation and substrate recognition. In: Molecular Biology Reports. 1997 ; Vol. 24, No. 1-2. pp. 39-44.
@article{1d745219af46452a96cf270055cfc648,
title = "The 26S-proteasome: Regulation and substrate recognition",
abstract = "There is extensive reprogramming of the ATPase regulators of the 26S proteasome before the programmed elimination of the abdominal intersegmental muscles (ISM) after eclosion in Manduca sexta [1]. This extensive ATPase reprogramming only occurs in ISM which are destined to die and not in flight muscle (FM). The MS73 ATPase also increases in the proleg retractor muscles which die at a developmentally different stage to ISM. The non-ATPase regulator S5a shows a similar increase to the ATPase regulators. We have cloned the Manduca SUG2 ATPase and shown that this ATPase is a component of the 26S proteasome. This ATPase shows a similar increase in concentration to the other ATPases in 26S proteasomes before muscle death. The SUG2 ATPase is also associated with other smaller complexes besides the 26S proteasome which act as activators of the 26S proteasome. Finally, in a yeast two-hybrid genetic screen we have identified a protein in human brain which interacts with the MS73 ATPase (and human S6). The interacting protein contains 6 ankyrin repeats and is co-immunoprecipitated with anti-MS73 antiserum after in vitro transcription/translation. The ankyrin repeat protein may interact with the MS73 ATPase as part of the substrate recognition process by the 26S proteasome. Many proteins degraded by the 26S proteasome contain ankyrin repeats, e.g. IkB and some cyclins: binding through ankyrin repeats to an ATPase regulator may complement protein ubiquitination and S5a binding as recognition signals by the 26S proteasome.",
keywords = "26S proteasome, ATPase, Programmed cell death, Regulators",
author = "Simon Dawson and Richard Hastings and Katsuhiko Takayanagi and Stuart Reynolds and P. Lőw and Michael Billett and {John Mayer}, R.",
year = "1997",
month = "3",
language = "English",
volume = "24",
pages = "39--44",
journal = "Molecular Biology Reports",
issn = "0301-4851",
publisher = "Springer Netherlands",
number = "1-2",

}

TY - JOUR

T1 - The 26S-proteasome

T2 - Regulation and substrate recognition

AU - Dawson, Simon

AU - Hastings, Richard

AU - Takayanagi, Katsuhiko

AU - Reynolds, Stuart

AU - Lőw, P.

AU - Billett, Michael

AU - John Mayer, R.

PY - 1997/3

Y1 - 1997/3

N2 - There is extensive reprogramming of the ATPase regulators of the 26S proteasome before the programmed elimination of the abdominal intersegmental muscles (ISM) after eclosion in Manduca sexta [1]. This extensive ATPase reprogramming only occurs in ISM which are destined to die and not in flight muscle (FM). The MS73 ATPase also increases in the proleg retractor muscles which die at a developmentally different stage to ISM. The non-ATPase regulator S5a shows a similar increase to the ATPase regulators. We have cloned the Manduca SUG2 ATPase and shown that this ATPase is a component of the 26S proteasome. This ATPase shows a similar increase in concentration to the other ATPases in 26S proteasomes before muscle death. The SUG2 ATPase is also associated with other smaller complexes besides the 26S proteasome which act as activators of the 26S proteasome. Finally, in a yeast two-hybrid genetic screen we have identified a protein in human brain which interacts with the MS73 ATPase (and human S6). The interacting protein contains 6 ankyrin repeats and is co-immunoprecipitated with anti-MS73 antiserum after in vitro transcription/translation. The ankyrin repeat protein may interact with the MS73 ATPase as part of the substrate recognition process by the 26S proteasome. Many proteins degraded by the 26S proteasome contain ankyrin repeats, e.g. IkB and some cyclins: binding through ankyrin repeats to an ATPase regulator may complement protein ubiquitination and S5a binding as recognition signals by the 26S proteasome.

AB - There is extensive reprogramming of the ATPase regulators of the 26S proteasome before the programmed elimination of the abdominal intersegmental muscles (ISM) after eclosion in Manduca sexta [1]. This extensive ATPase reprogramming only occurs in ISM which are destined to die and not in flight muscle (FM). The MS73 ATPase also increases in the proleg retractor muscles which die at a developmentally different stage to ISM. The non-ATPase regulator S5a shows a similar increase to the ATPase regulators. We have cloned the Manduca SUG2 ATPase and shown that this ATPase is a component of the 26S proteasome. This ATPase shows a similar increase in concentration to the other ATPases in 26S proteasomes before muscle death. The SUG2 ATPase is also associated with other smaller complexes besides the 26S proteasome which act as activators of the 26S proteasome. Finally, in a yeast two-hybrid genetic screen we have identified a protein in human brain which interacts with the MS73 ATPase (and human S6). The interacting protein contains 6 ankyrin repeats and is co-immunoprecipitated with anti-MS73 antiserum after in vitro transcription/translation. The ankyrin repeat protein may interact with the MS73 ATPase as part of the substrate recognition process by the 26S proteasome. Many proteins degraded by the 26S proteasome contain ankyrin repeats, e.g. IkB and some cyclins: binding through ankyrin repeats to an ATPase regulator may complement protein ubiquitination and S5a binding as recognition signals by the 26S proteasome.

KW - 26S proteasome

KW - ATPase

KW - Programmed cell death

KW - Regulators

UR - http://www.scopus.com/inward/record.url?scp=0031106312&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031106312&partnerID=8YFLogxK

M3 - Article

VL - 24

SP - 39

EP - 44

JO - Molecular Biology Reports

JF - Molecular Biology Reports

SN - 0301-4851

IS - 1-2

ER -