Thermostability of Two Cyanobacterial GrpE Thermosensors

Publication type:
Journal article
Metadata:
Autoren
  • S Barthel
  • E Rupprecht
  • D Schneider
DOI
10.1093/pcp/pcr116
eISSN
1471-9053
ISSN
0032-0781
Ausgabe der Veröffentlichung
10
Zeitschrift
Plant and Cell Physiology
Sprache
en
Online publication date
2011
Paginierung
1776 - 1785
Datum der Veröffentlichung
2011
Status
Published
Herausgeber
Oxford University Press (OUP)
Herausgeber URL
http://dx.doi.org/10.1093/pcp/pcr116
Datum der Datenerfassung
2017
Titel
Thermostability of Two Cyanobacterial GrpE Thermosensors
Ausgabe der Zeitschrift
52

Data source: Crossref

Other metadata sources:
Abstract
GrpE proteins act as co-chaperones for DnaK heat-shock proteins. The dimeric protein unfolds under heat stress conditions, which results in impaired interaction with a DnaK protein. Since interaction of GrpE with DnaK is crucial for the DnaK chaperone activity, GrpE proteins act as a thermosensor in bacteria. Here we have analyzed the thermostability and function of two GrpE homologs of the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and of the thermophilic cyanobacterium Thermosynechococcus elongatus BP1. While in Synechocystis an N-terminal helix pair of the GrpE dimer appears to be the thermosensing domain and mainly mediates GrpE dimerization, the C-terminal four-helix bundle is involved in additional stabilization of the dimeric structure. The four-helix bundle domain has a key role in the thermophilic cyanobacterium, since dimerization of the Thermosynechococcus protein appears to be mediated by the four-helix bundle domain, and melting of this domain is linked to monomerization of the GrpE protein. Thus, in two related cyanobacteria the GrpE thermosensing function might be mediated by different protein domains.
Addresses
  • Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität, Johann-Joachim-Becher-Weg 30, D-55128 Mainz, Germany.
Autoren
  • Sandra Barthel
  • Eva Rupprecht
  • Dirk Schneider
DOI
10.1093/pcp/pcr116
eISSN
1471-9053
Externe Identifier
  • PubMed Identifier: 21865302
Open access
false
ISSN
0032-0781
Ausgabe der Veröffentlichung
10
Zeitschrift
Plant & cell physiology
Schlüsselwörter
  • Cyanobacteria
  • Synechocystis
  • Escherichia coli
  • Bacterial Proteins
  • Heat-Shock Proteins
  • Cross-Linking Reagents
  • Circular Dichroism
  • Genetic Complementation Test
  • Temperature
  • Amino Acid Sequence
  • Protein Structure, Tertiary
  • Protein Binding
  • Sequence Homology, Amino Acid
  • Molecular Sequence Data
  • Protein Multimerization
  • Protein Stability
Sprache
eng
Medium
Print-Electronic
Online publication date
2011
Paginierung
1776 - 1785
Datum der Veröffentlichung
2011
Status
Published
Datum der Datenerfassung
2011
Titel
Thermostability of two cyanobacterial GrpE thermosensors.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
52

Data source: Europe PubMed Central

Abstract
GrpE proteins act as co-chaperones for DnaK heat-shock proteins. The dimeric protein unfolds under heat stress conditions, which results in impaired interaction with a DnaK protein. Since interaction of GrpE with DnaK is crucial for the DnaK chaperone activity, GrpE proteins act as a thermosensor in bacteria. Here we have analyzed the thermostability and function of two GrpE homologs of the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and of the thermophilic cyanobacterium Thermosynechococcus elongatus BP1. While in Synechocystis an N-terminal helix pair of the GrpE dimer appears to be the thermosensing domain and mainly mediates GrpE dimerization, the C-terminal four-helix bundle is involved in additional stabilization of the dimeric structure. The four-helix bundle domain has a key role in the thermophilic cyanobacterium, since dimerization of the Thermosynechococcus protein appears to be mediated by the four-helix bundle domain, and melting of this domain is linked to monomerization of the GrpE protein. Thus, in two related cyanobacteria the GrpE thermosensing function might be mediated by different protein domains.
Autoren
  • Sandra Barthel
  • Eva Rupprecht
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/21865302
DOI
10.1093/pcp/pcr116
eISSN
1471-9053
Ausgabe der Veröffentlichung
10
Zeitschrift
Plant Cell Physiol
Schlüsselwörter
  • Amino Acid Sequence
  • Bacterial Proteins
  • Circular Dichroism
  • Cross-Linking Reagents
  • Cyanobacteria
  • Escherichia coli
  • Genetic Complementation Test
  • Heat-Shock Proteins
  • Molecular Sequence Data
  • Protein Binding
  • Protein Multimerization
  • Protein Stability
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Synechocystis
  • Temperature
Sprache
eng
Country
Japan
Paginierung
1776 - 1785
PII
pcr116
Datum der Veröffentlichung
2011
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2012
Titel
Thermostability of two cyanobacterial GrpE thermosensors.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
52

Data source: PubMed

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