Small Residues Inhibit Homo-Dimerization of the Human Carbonic Anhydrase XII Transmembrane Domain
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- Florian Cymer
- Dirk Schneider
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000676756100001&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.3390/membranes11070512
- eISSN
- 2077-0375
- Externe Identifier
- Clarivate Analytics Document Solution ID: TO2NU
- PubMed Identifier: 34357162
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- MEMBRANES
- Schlüsselwörter
- carbonic anhydrase XII
- GxxxG
- transmembrane domain
- helix-helix interaction
- small amino acids
- interaction motif
- interaction propensity
- GALLEX
- Artikelnummer
- ARTN 512
- Datum der Veröffentlichung
- 2021
- Status
- Published
- Titel
- Small Residues Inhibit Homo-Dimerization of the Human Carbonic Anhydrase XII Transmembrane Domain
- Sub types
- Article
- Ausgabe der Zeitschrift
- 11
Data source: Web of Science (Lite)
- Other metadata sources:
-
- Abstract
- <jats:p>Amino acids with small side chains and motifs of small residues in a distance of four are rather abundant in human single-span transmembrane helices. While interaction of such helices appears to be common, the role of the small residues in mediating and/or stabilizing transmembrane helix oligomers remains mostly elusive. Yet, the mere existence of (small)xxx(small) motifs in transmembrane helices is frequently used to model dimeric TM helix structures. The single transmembrane helix of the human carbonic anhydrases XII contains a large number of amino acids with small side chains, and critical involvement of these small amino acids in dimerization of the transmembrane domain has been suggested. Using the GALLEX assay, we show here that the transmembrane domain indeed forms a strong transmembrane helix oligomer within a biological membrane. However, single or multiple mutations of small residue(s) to isoleucine almost always increased, rather than decreased, the interaction propensities. Reduction of helix flexibility and of protein–lipid contacts caused by a reduced lipid accessible surface area likely results in stabilization of helix–helix interactions within the membrane.</jats:p>
- Autoren
- Florian Cymer
- Dirk Schneider
- DOI
- 10.3390/membranes11070512
- eISSN
- 2077-0375
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- Membranes
- Sprache
- en
- Online publication date
- 2021
- Paginierung
- 512 - 512
- Status
- Published online
- Herausgeber
- MDPI AG
- Herausgeber URL
- http://dx.doi.org/10.3390/membranes11070512
- Datum der Datenerfassung
- 2021
- Titel
- Small Residues Inhibit Homo-Dimerization of the Human Carbonic Anhydrase XII Transmembrane Domain
- Ausgabe der Zeitschrift
- 11
Data source: Crossref
- Abstract
- Amino acids with small side chains and motifs of small residues in a distance of four are rather abundant in human single-span transmembrane helices. While interaction of such helices appears to be common, the role of the small residues in mediating and/or stabilizing transmembrane helix oligomers remains mostly elusive. Yet, the mere existence of (small)xxx(small) motifs in transmembrane helices is frequently used to model dimeric TM helix structures. The single transmembrane helix of the human carbonic anhydrases XII contains a large number of amino acids with small side chains, and critical involvement of these small amino acids in dimerization of the transmembrane domain has been suggested. Using the GALLEX assay, we show here that the transmembrane domain indeed forms a strong transmembrane helix oligomer within a biological membrane. However, single or multiple mutations of small residue(s) to isoleucine almost always increased, rather than decreased, the interaction propensities. Reduction of helix flexibility and of protein-lipid contacts caused by a reduced lipid accessible surface area likely results in stabilization of helix-helix interactions within the membrane.
- Addresses
- Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.
- Autoren
- Florian Cymer
- Dirk Schneider
- DOI
- 10.3390/membranes11070512
- eISSN
- 2077-0375
- Externe Identifier
- PubMed Identifier: 34357162
- PubMed Central ID: PMC8307134
- Funding acknowledgements
- state of Rhineland-Palatinate: DynaMem
- Deutsche Forschungsgemeinschaft: SCHN 690/2-3
- Open access
- true
- ISSN
- 2077-0375
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- Membranes
- Sprache
- eng
- Medium
- Electronic
- Online publication date
- 2021
- Open access status
- Open Access
- Paginierung
- 512
- Datum der Veröffentlichung
- 2021
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2021
- Titel
- Small Residues Inhibit Homo-Dimerization of the Human Carbonic Anhydrase XII Transmembrane Domain.
- Sub types
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 11
Files
https://www.mdpi.com/2077-0375/11/7/512/pdf?version=1625657875 https://europepmc.org/articles/PMC8307134?pdf=render
Data source: Europe PubMed Central
- Abstract
- Amino acids with small side chains and motifs of small residues in a distance of four are rather abundant in human single-span transmembrane helices. While interaction of such helices appears to be common, the role of the small residues in mediating and/or stabilizing transmembrane helix oligomers remains mostly elusive. Yet, the mere existence of (small)xxx(small) motifs in transmembrane helices is frequently used to model dimeric TM helix structures. The single transmembrane helix of the human carbonic anhydrases XII contains a large number of amino acids with small side chains, and critical involvement of these small amino acids in dimerization of the transmembrane domain has been suggested. Using the GALLEX assay, we show here that the transmembrane domain indeed forms a strong transmembrane helix oligomer within a biological membrane. However, single or multiple mutations of small residue(s) to isoleucine almost always increased, rather than decreased, the interaction propensities. Reduction of helix flexibility and of protein-lipid contacts caused by a reduced lipid accessible surface area likely results in stabilization of helix-helix interactions within the membrane.
- Date of acceptance
- 2021
- Autoren
- Florian Cymer
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/34357162
- DOI
- 10.3390/membranes11070512
- Externe Identifier
- PubMed Central ID: PMC8307134
- Funding acknowledgements
- Deutsche Forschungsgemeinschaft: SCHN 690/2-3
- state of Rhineland-Palatinate: DynaMem
- ISSN
- 2077-0375
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- Membranes (Basel)
- Schlüsselwörter
- GALLEX
- GxxxG
- carbonic anhydrase XII
- helix–helix interaction
- interaction motif
- interaction propensity
- small amino acids
- transmembrane domain
- Sprache
- eng
- Country
- Switzerland
- PII
- membranes11070512
- Datum der Veröffentlichung
- 2021
- Status
- Published online
- Titel
- Small Residues Inhibit Homo-Dimerization of the Human Carbonic Anhydrase XII Transmembrane Domain.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 11
Data source: PubMed
- Author's licence
- CC-BY
- Autoren
- Florian Cymer
- Dirk Schneider
- Hosting institution
- Universitätsbibliothek Mainz
- Sammlungen
- JGU-Publikationen
- Resource version
- Published version
- DOI
- 10.3390/membranes11070512
- Funding acknowledgements
- Open Access-Publizieren Universität Mainz / Universitätsmedizin Mainz
- File(s) embargoed
- false
- Open access
- true
- ISSN
- 2077-0375
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- Membranes
- Schlüsselwörter
- 540 Chemie
- 540 Chemistry and allied sciences
- 570 Biowissenschaften
- 570 Life sciences
- Sprache
- eng
- Open access status
- Open Access
- Paginierung
- 512
- Datum der Veröffentlichung
- 2021
- Public URL
- https://openscience.ub.uni-mainz.de/handle/20.500.12030/6525
- Herausgeber
- MDPI
- Herausgeber URL
- https://doi.org/10.3390/membranes11070512
- Datum der Datenerfassung
- 2021
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2021
- Zugang
- Public
- Titel
- Small residues inhibit homo-dimerization of the human carbonic anhydrase XII transmembrane domain
- Ausgabe der Zeitschrift
- 11
Files
cymer_florian-small_residues-20211115121527126.pdf
Data source: OPENSCIENCE.UB
- Beziehungen:
- Property of