Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- Noreen Klein
- Nadja Hellmann
- Dirk Schneider
- DOI
- 10.1016/j.bpj.2015.06.063
- ISSN
- 0006-3495
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- Biophysical Journal
- Sprache
- en
- Paginierung
- 722 - 731
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Herausgeber
- Elsevier BV
- Herausgeber URL
- http://dx.doi.org/10.1016/j.bpj.2015.06.063
- Datum der Datenerfassung
- 2019
- Titel
- Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF
- Ausgabe der Zeitschrift
- 109
Data source: Crossref
- Other metadata sources:
-
- Abstract
- The structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact, we found that GlpF activity was severely affected by negatively charged lipids regardless of the exact chemical nature of the lipid headgroup, whereas GlpF was not sensitive to changes in the lateral membrane pressure. These observations illustrate a potential mechanism by which the activity of an α-helical membrane protein is modulated by the negative charge density around the protein.
- Addresses
- Institut für Pharmazie und Biochemie, Johannes Gutenberg Universität Mainz, Mainz, Germany.
- Autoren
- Noreen Klein
- Nadja Hellmann
- Dirk Schneider
- DOI
- 10.1016/j.bpj.2015.06.063
- eISSN
- 1542-0086
- Externe Identifier
- PubMed Identifier: 26287624
- PubMed Central ID: PMC4547167
- Open access
- false
- ISSN
- 0006-3495
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- Biophysical journal
- Schlüsselwörter
- Escherichia coli
- Anions
- Lipids
- Aquaporins
- Escherichia coli Proteins
- Liposomes
- Sprache
- eng
- Medium
- Paginierung
- 722 - 731
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Datum der Datenerfassung
- 2015
- Titel
- Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 109
Files
http://www.cell.com/article/S0006349515006773/pdf https://europepmc.org/articles/PMC4547167?pdf=render
Data source: Europe PubMed Central
- Abstract
- The structure and composition of a biological membrane can severely influence the activity of membrane-embedded proteins. Here, we show that the E. coli aquaglyceroporin GlpF has only little activity in lipid bilayers formed from native E. coli lipids. Thus, at first glance, GlpF appears to not be optimized for its natural membrane environment. In fact, we found that GlpF activity was severely affected by negatively charged lipids regardless of the exact chemical nature of the lipid headgroup, whereas GlpF was not sensitive to changes in the lateral membrane pressure. These observations illustrate a potential mechanism by which the activity of an α-helical membrane protein is modulated by the negative charge density around the protein.
- Date of acceptance
- 2015
- Autoren
- Noreen Klein
- Nadja Hellmann
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/26287624
- DOI
- 10.1016/j.bpj.2015.06.063
- eISSN
- 1542-0086
- Externe Identifier
- PubMed Central ID: PMC4547167
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- Biophys J
- Schlüsselwörter
- Anions
- Aquaporins
- Escherichia coli
- Escherichia coli Proteins
- Lipids
- Liposomes
- Sprache
- eng
- Country
- United States
- Paginierung
- 722 - 731
- PII
- S0006-3495(15)00677-3
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2016
- Titel
- Anionic Lipids Modulate the Activity of the Aquaglyceroporin GlpF.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 109
Data source: PubMed
- Beziehungen:
- Property of