A Single Glutamate Residue Controls the Oligomerization, Function, and Stability of the Aquaglyceroporin GlpF

Publikationstyp:
Zeitschriftenaufsatz
Metadaten:
Autoren
  • Florian Cymer
  • Dirk Schneider
DOI
10.1021/bi901660t
eISSN
1520-4995
ISSN
0006-2960
Ausgabe der Veröffentlichung
2
Zeitschrift
Biochemistry
Sprache
en
Online publication date
2009
Paginierung
279 - 286
Datum der Veröffentlichung
2010
Status
Published
Herausgeber
American Chemical Society (ACS)
Herausgeber URL
http://dx.doi.org/10.1021/bi901660t
Datum der Datenerfassung
2023
Titel
A Single Glutamate Residue Controls the Oligomerization, Function, and Stability of the Aquaglyceroporin GlpF
Ausgabe der Zeitschrift
49

Datenquelle: Crossref

Andere Metadatenquellen:
Abstract
Like many other alpha-helical membrane proteins, the monomeric Escherichia coli aquaglyceroporin GlpF associates within cellular membranes and forms higher-order oligomeric structures. A potential impact of the oligomeric state on the protein function remains enigmatic. We have analyzed the role of residues W42 and E43 in the oligomerization of the E. coli GlpF protein in vitro and in vivo. In contrast to W42, the polar glutamate residue at position 43 appears to be critical for oligomerization. While other polar residues can substitute for the function of E43, replacement of E43 with alanine results in a greatly reduced GlpF oligomerization propensity. The reduced interaction propensity of GlpF E43A correlates with an impaired in vivo function as well as a decreased in vivo stability. Therefore, E43 is critical for the proper oligomerization of GlpF, and protein oligomerization appears to be crucial for the channel function as well as for the in vivo stability of the protein.
Addresses
  • Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität Freiburg,Stefan-Meier-Strasse 17, 79104 Freiburg, Germany.
Autoren
  • Florian Cymer
  • Dirk Schneider
DOI
10.1021/bi901660t
eISSN
1520-4995
Externe Identifier
  • PubMed Identifier: 20000688
Open access
false
ISSN
0006-2960
Ausgabe der Veröffentlichung
2
Zeitschrift
Biochemistry
Schlüsselwörter
  • Cell Membrane
  • Escherichia coli
  • Glutamic Acid
  • Tryptophan
  • Oligopeptides
  • Bacterial Proteins
  • Membrane Proteins
  • Crystallography, X-Ray
  • Cloning, Molecular
  • Polymerase Chain Reaction
  • Drug Stability
  • Gene Amplification
  • Protein Conformation
  • Plasmids
  • Models, Molecular
  • Aquaglyceroporins
Sprache
eng
Medium
Print
Paginierung
279 - 286
Datum der Veröffentlichung
2010
Status
Published
Datum der Datenerfassung
2009
Titel
A single glutamate residue controls the oligomerization, function, and stability of the aquaglyceroporin GlpF.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
49

Datenquelle: Europe PubMed Central

Abstract
Like many other alpha-helical membrane proteins, the monomeric Escherichia coli aquaglyceroporin GlpF associates within cellular membranes and forms higher-order oligomeric structures. A potential impact of the oligomeric state on the protein function remains enigmatic. We have analyzed the role of residues W42 and E43 in the oligomerization of the E. coli GlpF protein in vitro and in vivo. In contrast to W42, the polar glutamate residue at position 43 appears to be critical for oligomerization. While other polar residues can substitute for the function of E43, replacement of E43 with alanine results in a greatly reduced GlpF oligomerization propensity. The reduced interaction propensity of GlpF E43A correlates with an impaired in vivo function as well as a decreased in vivo stability. Therefore, E43 is critical for the proper oligomerization of GlpF, and protein oligomerization appears to be crucial for the channel function as well as for the in vivo stability of the protein.
Autoren
  • Florian Cymer
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/20000688
DOI
10.1021/bi901660t
eISSN
1520-4995
Ausgabe der Veröffentlichung
2
Zeitschrift
Biochemistry
Schlüsselwörter
  • Aquaglyceroporins
  • Bacterial Proteins
  • Cell Membrane
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Drug Stability
  • Escherichia coli
  • Gene Amplification
  • Glutamic Acid
  • Membrane Proteins
  • Models, Molecular
  • Oligopeptides
  • Plasmids
  • Polymerase Chain Reaction
  • Protein Conformation
  • Tryptophan
Sprache
eng
Country
United States
Paginierung
279 - 286
Datum der Veröffentlichung
2010
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2010
Titel
A single glutamate residue controls the oligomerization, function, and stability of the aquaglyceroporin GlpF.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
49

Datenquelle: PubMed

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