Please use this identifier to cite or link to this item:
http://doi.org/10.25358/openscience-769Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Klein, Noreen | - |
| dc.contributor.author | Trefz, Margareta | - |
| dc.contributor.author | Schneider, Dirk | - |
| dc.date.accessioned | 2019-04-15T10:15:13Z | - |
| dc.date.available | 2019-04-15T12:15:13Z | - |
| dc.date.issued | 2019 | - |
| dc.identifier.uri | https://openscience.ub.uni-mainz.de/handle/20.500.12030/771 | - |
| dc.description.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. | en_GB |
| dc.description.sponsorship | DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin | - |
| dc.language.iso | eng | - |
| dc.rights | CC BY | de_DE |
| dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | - |
| dc.subject.ddc | 570 Biowissenschaften | de_DE |
| dc.subject.ddc | 570 Life sciences | en_GB |
| dc.title | Covalently linking oligomerization-impaired GlpF protomers does not completely re-establish wild-type channel activity | en_GB |
| dc.type | Zeitschriftenaufsatz | de_DE |
| dc.identifier.urn | urn:nbn:de:hebis:77-publ-590311 | - |
| dc.identifier.doi | http://doi.org/10.25358/openscience-769 | - |
| jgu.type.dinitype | article | - |
| jgu.type.version | Published version | en_GB |
| jgu.type.resource | Text | - |
| jgu.organisation.department | FB 09 Chemie, Pharmazie u. Geowissensch. | - |
| jgu.organisation.number | 7950 | - |
| jgu.organisation.name | Johannes Gutenberg-Universität Mainz | - |
| jgu.rights.accessrights | openAccess | - |
| jgu.journal.title | International journal of molecular sciences | - |
| jgu.journal.volume | 20 | - |
| jgu.journal.issue | 4 | - |
| jgu.pages.alternative | Art. 927 | - |
| jgu.publisher.year | 2019 | - |
| jgu.publisher.name | Molecular Diversity Preservation International | - |
| jgu.publisher.place | Basel | - |
| jgu.publisher.uri | http://dx.doi.org/10.3390/ijms20040927 | - |
| jgu.publisher.issn | 1422-0067 | - |
| jgu.organisation.place | Mainz | - |
| jgu.subject.ddccode | 570 | - |
| opus.date.accessioned | 2019-04-15T10:15:13Z | - |
| opus.date.modified | 2019-04-15T10:15:49Z | - |
| opus.date.available | 2019-04-15T12:15:13 | - |
| opus.subject.dfgcode | 00-000 | - |
| opus.organisation.string | FB 09: Chemie, Pharmazie und Geowissenschaften: Institut für Pharmazie und Biochemie | de_DE |
| opus.identifier.opusid | 59031 | - |
| opus.institute.number | 0910 | - |
| opus.metadataonly | false | - |
| opus.type.contenttype | Keine | de_DE |
| opus.type.contenttype | None | en_GB |
| opus.affiliated | Trefz, Margareta | - |
| opus.affiliated | Schneider, Dirk | - |
| jgu.publisher.doi | 10.3390/ijms20040927 | |
| jgu.organisation.ror | https://ror.org/023b0x485 | |
| Appears in collections: | JGU-Publikationen | |
