Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Noreen Klein
- Margareta Trefz
- Dirk Schneider
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000460805400135&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.3390/ijms20040927
- Externe Identifier
- Clarivate Analytics Document Solution ID: HO3FO
- PubMed Identifier: 30791644
- ISSN
- 1422-0067
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Schlüsselwörter
- aquaglyceroporin
- covalent linkage
- GlpF
- homooligomer
- membrane protein
- protein folding
- tetramer
- interaction
- Artikelnummer
- ARTN 927
- Datum der Veröffentlichung
- 2019
- Status
- Published
- Titel
- Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity
- Sub types
- Article
- Ausgabe der Zeitschrift
- 20
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Abstract
- <jats:p>Integral membrane proteins of the aquaporin family facilitate rapid water flux across cellular membranes in all domains of life. Although the water-conducting pore is clearly defined in an aquaporin monomer, all aquaporins assemble into stable tetramers. In order to investigate the role of protomer–protomer interactions, we analyzed the activity of heterotetramers containing increasing fractions of mutated monomers, which have an impaired oligomerization propensity and activity. In order to enforce interaction between the protomers, we designed and analyzed a genetically fused homotetramer of GlpF, the aquaglyceroporin of the bacterium Escherichia coli (E. coli). However, increasing fractions of the oligomerization-impaired mutant GlpF E43A affected the activity of the GlpF heterotetramer in a nearly linear manner, indicating that the reduced protein activity, caused by the introduced mutations, cannot be fully compensated by simply covalently linking the monomers. Taken together, the results underline the importance of exactly positioned monomer–monomer contacts in an assembled GlpF tetramer.</jats:p>
- Autoren
- Noreen Klein
- Margareta Trefz
- Dirk Schneider
- DOI
- 10.3390/ijms20040927
- eISSN
- 1422-0067
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- International Journal of Molecular Sciences
- Sprache
- en
- Online publication date
- 2019
- Paginierung
- 927 - 927
- Status
- Published online
- Herausgeber
- MDPI AG
- Herausgeber URL
- http://dx.doi.org/10.3390/ijms20040927
- Datum der Datenerfassung
- 2022
- Titel
- Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity
- Ausgabe der Zeitschrift
- 20
Datenquelle: Crossref
- Abstract
- Integral membrane proteins of the aquaporin family facilitate rapid water flux across cellular membranes in all domains of life. Although the water-conducting pore is clearly defined in an aquaporin monomer, all aquaporins assemble into stable tetramers. In order to investigate the role of protomer⁻protomer interactions, we analyzed the activity of heterotetramers containing increasing fractions of mutated monomers, which have an impaired oligomerization propensity and activity. In order to enforce interaction between the protomers, we designed and analyzed a genetically fused homotetramer of GlpF, the aquaglyceroporin of the bacterium <i>Escherichia coli</i> (<i>E. coli</i>). However, increasing fractions of the oligomerization-impaired mutant GlpF E43A affected the activity of the GlpF heterotetramer in a nearly linear manner, indicating that the reduced protein activity, caused by the introduced mutations, cannot be fully compensated by simply covalently linking the monomers. Taken together, the results underline the importance of exactly positioned monomer⁻monomer contacts in an assembled GlpF tetramer.
- Addresses
- Johannes Gutenberg-University Mainz, Institute of Pharmacy and Biochemistry, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany. noreen-klein@freenet.de.
- Autoren
- Noreen Klein
- Margareta Trefz
- Dirk Schneider
- DOI
- 10.3390/ijms20040927
- eISSN
- 1422-0067
- Externe Identifier
- PubMed Identifier: 30791644
- PubMed Central ID: PMC6412381
- Funding acknowledgements
- German Chemical Industry fund: N/A
- Research Center for Complex Materials (COMATT): N/A
- Stiftung Rheinland-Pfalz für Innovation: N/A
- Open access
- true
- ISSN
- 1422-0067
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- International journal of molecular sciences
- Schlüsselwörter
- Bacterial Outer Membrane Proteins
- Aquaporins
- Escherichia coli Proteins
- Recombinant Fusion Proteins
- Cloning, Molecular
- Gene Expression
- Structure-Activity Relationship
- Biological Transport
- Mutation
- Protein Multimerization
- Sprache
- eng
- Medium
- Electronic
- Online publication date
- 2019
- Open access status
- Open Access
- Paginierung
- E927
- Datum der Veröffentlichung
- 2019
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2019
- Titel
- Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity.
- Sub types
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 20
Files
https://www.mdpi.com/1422-0067/20/4/927/pdf?version=1550667359 https://europepmc.org/articles/PMC6412381?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- Integral membrane proteins of the aquaporin family facilitate rapid water flux across cellular membranes in all domains of life. Although the water-conducting pore is clearly defined in an aquaporin monomer, all aquaporins assemble into stable tetramers. In order to investigate the role of protomer⁻protomer interactions, we analyzed the activity of heterotetramers containing increasing fractions of mutated monomers, which have an impaired oligomerization propensity and activity. In order to enforce interaction between the protomers, we designed and analyzed a genetically fused homotetramer of GlpF, the aquaglyceroporin of the bacterium Escherichia coli (E. coli). However, increasing fractions of the oligomerization-impaired mutant GlpF E43A affected the activity of the GlpF heterotetramer in a nearly linear manner, indicating that the reduced protein activity, caused by the introduced mutations, cannot be fully compensated by simply covalently linking the monomers. Taken together, the results underline the importance of exactly positioned monomer⁻monomer contacts in an assembled GlpF tetramer.
- Date of acceptance
- 2019
- Autoren
- Noreen Klein
- Margareta Trefz
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/30791644
- DOI
- 10.3390/ijms20040927
- eISSN
- 1422-0067
- Externe Identifier
- PubMed Central ID: PMC6412381
- Funding acknowledgements
- Stiftung Rheinland-Pfalz für Innovation: N/A
- German Chemical Industry fund: N/A
- Research Center for Complex Materials (COMATT): N/A
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- Int J Mol Sci
- Schlüsselwörter
- GlpF
- aquaglyceroporin
- covalent linkage
- homooligomer
- interaction
- membrane protein
- protein folding
- tetramer
- Aquaporins
- Bacterial Outer Membrane Proteins
- Biological Transport
- Cloning, Molecular
- Escherichia coli Proteins
- Gene Expression
- Mutation
- Protein Multimerization
- Recombinant Fusion Proteins
- Structure-Activity Relationship
- Sprache
- eng
- Country
- Switzerland
- PII
- ijms20040927
- Datum der Veröffentlichung
- 2019
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2019
- Titel
- Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 20
Datenquelle: PubMed
- Author's licence
- CC-BY
- Autoren
- Noreen Klein
- Margareta Trefz
- Dirk Schneider
- Hosting institution
- Universitätsbibliothek Mainz
- Sammlungen
- JGU-Publikationen
- Resource version
- Published version
- URN
- urn:nbn:de:hebis:77-publ-590311
- DOI
- 10.3390/ijms20040927
- Funding acknowledgements
- DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin
- File(s) embargoed
- false
- Open access
- true
- ISSN
- 1422-0067
- Ausgabe der Veröffentlichung
- 4
- Zeitschrift
- International journal of molecular sciences
- Schlüsselwörter
- 570 Biowissenschaften
- 570 Life sciences
- Sprache
- eng
- Open access status
- Open Access
- Paginierung
- Art. 927
- Datum der Veröffentlichung
- 2019
- Public URL
- https://openscience.ub.uni-mainz.de/handle/20.500.12030/771
- Herausgeber
- Molecular Diversity Preservation International
- Herausgeber URL
- http://dx.doi.org/10.3390/ijms20040927
- Datum der Datenerfassung
- 2019
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2019
- Zugang
- Public
- Titel
- Covalently linking oligomerization-impaired GlpF protomers does not completely re-establish wild-type channel activity
- Ausgabe der Zeitschrift
- 20
Files
59031.pdf
Datenquelle: OPENSCIENCE.UB
- Beziehungen:
- Eigentum von