Pressure activation of the chaperone function of small heat shock proteins.

F. Tölgyesi, C. S. Böde, L. Smeller, D. R. Kim, K. K. Kim, K. Heremans, J. Fidy

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Small heat shock proteins play an important role in the stress response of cells and in several other cellular functions. They possess chaperone-like activity; i.e. they can bind and protect damaged proteins from aggregation and maintain them in a folding-competent state. Two members of this family were investigated in this work: bovine alpha-crystallin and heat shock protein (HSP)16.5 from the thermophilic archaebacteria Methanococcus jannaschii. We reported earlier the enhancement of chaperone potency of alpha-crystallin by high pressure. We now report the completion of the work with results on HSP16.5. The chaperone potency of both proteins can be enhanced significantly by applying high pressure. Evidence by light scattering, Fourier transform infrared (FT-IR) and tryptophan fluorescence experiments show that while the secondary and tertiary structure of these proteins are not influenced by high pressure, their quatemary structure becomes affected: H bonds between subunits are weakened or broken, tryptophan environments become more polar, oligomers dissociate to some extent. We conclude that the oligomeric structure of both proteins is loosened, resulting in stronger dynamics and in more accessible hydrophobic surfaces. These properties lead to increased chaperone potency.

Original languageEnglish
Pages (from-to)361-369
Number of pages9
JournalCellular and Molecular Biology
Volume50
Issue number4
Publication statusPublished - Jun 2004

Fingerprint

Small Heat-Shock Proteins
alpha-Crystallins
Chemical activation
Pressure
Tryptophan
Methanocaldococcus
Secondary Protein Structure
Proteins
Archaea
Fourier Analysis
Tertiary Protein Structure
Fluorescence
Oligomers
Light scattering
Light
Fourier transforms
Agglomeration
Infrared radiation
Experiments

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

Cite this

Pressure activation of the chaperone function of small heat shock proteins. / Tölgyesi, F.; Böde, C. S.; Smeller, L.; Kim, D. R.; Kim, K. K.; Heremans, K.; Fidy, J.

In: Cellular and Molecular Biology, Vol. 50, No. 4, 06.2004, p. 361-369.

Research output: Contribution to journalArticle

Tölgyesi, F. ; Böde, C. S. ; Smeller, L. ; Kim, D. R. ; Kim, K. K. ; Heremans, K. ; Fidy, J. / Pressure activation of the chaperone function of small heat shock proteins. In: Cellular and Molecular Biology. 2004 ; Vol. 50, No. 4. pp. 361-369.
@article{bec95992f8fd4efb9cbcefb374c2fbc1,
title = "Pressure activation of the chaperone function of small heat shock proteins.",
abstract = "Small heat shock proteins play an important role in the stress response of cells and in several other cellular functions. They possess chaperone-like activity; i.e. they can bind and protect damaged proteins from aggregation and maintain them in a folding-competent state. Two members of this family were investigated in this work: bovine alpha-crystallin and heat shock protein (HSP)16.5 from the thermophilic archaebacteria Methanococcus jannaschii. We reported earlier the enhancement of chaperone potency of alpha-crystallin by high pressure. We now report the completion of the work with results on HSP16.5. The chaperone potency of both proteins can be enhanced significantly by applying high pressure. Evidence by light scattering, Fourier transform infrared (FT-IR) and tryptophan fluorescence experiments show that while the secondary and tertiary structure of these proteins are not influenced by high pressure, their quatemary structure becomes affected: H bonds between subunits are weakened or broken, tryptophan environments become more polar, oligomers dissociate to some extent. We conclude that the oligomeric structure of both proteins is loosened, resulting in stronger dynamics and in more accessible hydrophobic surfaces. These properties lead to increased chaperone potency.",
author = "F. T{\"o}lgyesi and B{\"o}de, {C. S.} and L. Smeller and Kim, {D. R.} and Kim, {K. K.} and K. Heremans and J. Fidy",
year = "2004",
month = "6",
language = "English",
volume = "50",
pages = "361--369",
journal = "Cellular and Molecular Biology",
issn = "0145-5680",
publisher = "Cellular and Molecular Biology Association",
number = "4",

}

TY - JOUR

T1 - Pressure activation of the chaperone function of small heat shock proteins.

AU - Tölgyesi, F.

AU - Böde, C. S.

AU - Smeller, L.

AU - Kim, D. R.

AU - Kim, K. K.

AU - Heremans, K.

AU - Fidy, J.

PY - 2004/6

Y1 - 2004/6

N2 - Small heat shock proteins play an important role in the stress response of cells and in several other cellular functions. They possess chaperone-like activity; i.e. they can bind and protect damaged proteins from aggregation and maintain them in a folding-competent state. Two members of this family were investigated in this work: bovine alpha-crystallin and heat shock protein (HSP)16.5 from the thermophilic archaebacteria Methanococcus jannaschii. We reported earlier the enhancement of chaperone potency of alpha-crystallin by high pressure. We now report the completion of the work with results on HSP16.5. The chaperone potency of both proteins can be enhanced significantly by applying high pressure. Evidence by light scattering, Fourier transform infrared (FT-IR) and tryptophan fluorescence experiments show that while the secondary and tertiary structure of these proteins are not influenced by high pressure, their quatemary structure becomes affected: H bonds between subunits are weakened or broken, tryptophan environments become more polar, oligomers dissociate to some extent. We conclude that the oligomeric structure of both proteins is loosened, resulting in stronger dynamics and in more accessible hydrophobic surfaces. These properties lead to increased chaperone potency.

AB - Small heat shock proteins play an important role in the stress response of cells and in several other cellular functions. They possess chaperone-like activity; i.e. they can bind and protect damaged proteins from aggregation and maintain them in a folding-competent state. Two members of this family were investigated in this work: bovine alpha-crystallin and heat shock protein (HSP)16.5 from the thermophilic archaebacteria Methanococcus jannaschii. We reported earlier the enhancement of chaperone potency of alpha-crystallin by high pressure. We now report the completion of the work with results on HSP16.5. The chaperone potency of both proteins can be enhanced significantly by applying high pressure. Evidence by light scattering, Fourier transform infrared (FT-IR) and tryptophan fluorescence experiments show that while the secondary and tertiary structure of these proteins are not influenced by high pressure, their quatemary structure becomes affected: H bonds between subunits are weakened or broken, tryptophan environments become more polar, oligomers dissociate to some extent. We conclude that the oligomeric structure of both proteins is loosened, resulting in stronger dynamics and in more accessible hydrophobic surfaces. These properties lead to increased chaperone potency.

UR - http://www.scopus.com/inward/record.url?scp=21644448482&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=21644448482&partnerID=8YFLogxK

M3 - Article

VL - 50

SP - 361

EP - 369

JO - Cellular and Molecular Biology

JF - Cellular and Molecular Biology

SN - 0145-5680

IS - 4

ER -