Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Abstract
- <jats:p>Genetic assays capable of measuring the propensity of transmembrane helices to oligomerize within the cytoplasmic membrane of the bacterium <jats:italic>E. coli</jats:italic> are frequently used when sequence-specificity in transmembrane helix-helix interactions is investigated. In the present study, dimerization of the well-investigated wild-type and G83I-mutated transmembrane helix of the human glycophorin A protein was studied. Gradual prolongation of the transmembrane helix at the C-terminus with Leu residues lead to pronounced changes in the dimerization propensity when measured with the TOXCAT assay. Thus, besides sequence specificity, hydrophobic mismatch between the hydrophobic core of a studied transmembrane helix and the <jats:italic>E. coli</jats:italic> membrane can impact the oligomerization propensity of a transmembrane helix. This suggests that the results of genetic assays aiming at determining interactions of heterologous transmembrane helices within the <jats:italic>E. coli</jats:italic> membrane do not necessarily solely reflect sequence specificity in transmembrane helix-helix interactions, but might be additionally modulated by topological and structural effects caused by hydrophobic mismatch.</jats:p>
- Autoren
- Nadja Hellmann
- Dirk Schneider
- DOI
- 10.3389/fchem.2022.1049310
- eISSN
- 2296-2646
- Zeitschrift
- Frontiers in Chemistry
- Online publication date
- 2022
- Status
- Published online
- Herausgeber
- Frontiers Media SA
- Herausgeber URL
- http://dx.doi.org/10.3389/fchem.2022.1049310
- Datum der Datenerfassung
- 2022
- Titel
- Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay
- Ausgabe der Zeitschrift
- 10
Datenquelle: Crossref
- Andere Metadatenquellen:
-
- Abstract
- Genetic assays capable of measuring the propensity of transmembrane helices to oligomerize within the cytoplasmic membrane of the bacterium <i>E. coli</i> are frequently used when sequence-specificity in transmembrane helix-helix interactions is investigated. In the present study, dimerization of the well-investigated wild-type and G83I-mutated transmembrane helix of the human glycophorin A protein was studied. Gradual prolongation of the transmembrane helix at the C-terminus with Leu residues lead to pronounced changes in the dimerization propensity when measured with the TOXCAT assay. Thus, besides sequence specificity, hydrophobic mismatch between the hydrophobic core of a studied transmembrane helix and the <i>E. coli</i> membrane can impact the oligomerization propensity of a transmembrane helix. This suggests that the results of genetic assays aiming at determining interactions of heterologous transmembrane helices within the <i>E. coli</i> membrane do not necessarily solely reflect sequence specificity in transmembrane helix-helix interactions, but might be additionally modulated by topological and structural effects caused by hydrophobic mismatch.
- Addresses
- Department Chemie-Biochemie, Johannes Gutenberg-Universität Mainz, Mainz, Germany.
- Autoren
- Nadja Hellmann
- Dirk Schneider
- DOI
- 10.3389/fchem.2022.1049310
- eISSN
- 2296-2646
- Externe Identifier
- PubMed Identifier: 36518980
- PubMed Central ID: PMC9742436
- Open access
- true
- ISSN
- 2296-2646
- Zeitschrift
- Frontiers in chemistry
- Sprache
- eng
- Medium
- Electronic-eCollection
- Online publication date
- 2022
- Open access status
- Open Access
- Paginierung
- 1049310
- Datum der Veröffentlichung
- 2022
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2022
- Titel
- Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay.
- Sub types
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 10
Files
https://www.frontiersin.org/articles/10.3389/fchem.2022.1049310/pdf https://europepmc.org/articles/PMC9742436?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- Genetic assays capable of measuring the propensity of transmembrane helices to oligomerize within the cytoplasmic membrane of the bacterium E. coli are frequently used when sequence-specificity in transmembrane helix-helix interactions is investigated. In the present study, dimerization of the well-investigated wild-type and G83I-mutated transmembrane helix of the human glycophorin A protein was studied. Gradual prolongation of the transmembrane helix at the C-terminus with Leu residues lead to pronounced changes in the dimerization propensity when measured with the TOXCAT assay. Thus, besides sequence specificity, hydrophobic mismatch between the hydrophobic core of a studied transmembrane helix and the E. coli membrane can impact the oligomerization propensity of a transmembrane helix. This suggests that the results of genetic assays aiming at determining interactions of heterologous transmembrane helices within the E. coli membrane do not necessarily solely reflect sequence specificity in transmembrane helix-helix interactions, but might be additionally modulated by topological and structural effects caused by hydrophobic mismatch.
- Date of acceptance
- 2022
- Autoren
- Nadja Hellmann
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/36518980
- DOI
- 10.3389/fchem.2022.1049310
- Externe Identifier
- PubMed Central ID: PMC9742436
- ISSN
- 2296-2646
- Zeitschrift
- Front Chem
- Schlüsselwörter
- GpA
- TOXCAT
- biological assay
- dimerization
- hydrophobic mismatch
- protein folding
- transmembrane helix
- Sprache
- eng
- Country
- Switzerland
- Paginierung
- 1049310
- PII
- 1049310
- Datum der Veröffentlichung
- 2022
- Status
- Published online
- Titel
- Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 10
Datenquelle: PubMed
- Author's licence
- CC-BY
- Autoren
- Nadja Hellmann
- Dirk Schneider
- Hosting institution
- Universitätsbibliothek Mainz
- Sammlungen
- DFG-491381577-G
- Resource version
- Published version
- DOI
- 10.3389/fchem.2022.1049310
- Funding acknowledgements
- Gefördert durch die Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 491381577
- File(s) embargoed
- false
- Open access
- true
- ISSN
- 2296-2646
- Zeitschrift
- Frontiers in chemistry
- Schlüsselwörter
- 540 Chemie
- 540 Chemistry and allied sciences
- Sprache
- eng
- Open access status
- Open Access
- Paginierung
- 1049310
- Datum der Veröffentlichung
- 2022
- Public URL
- https://openscience.ub.uni-mainz.de/handle/20.500.12030/8476
- Herausgeber
- Frontiers
- Datum der Datenerfassung
- 2022
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2022
- Zugang
- Public
- Titel
- Hydrophobic mismatch and sequence specificity compete when transmembrane helix-helix interactions are measured with the TOXCAT assay
- Ausgabe der Zeitschrift
- 10
Files
hydrophobic_mismatch_and_sequ-20221201122454514.pdf
Datenquelle: OPENSCIENCE.UB