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Authors: Klein, Noreen
Trefz, Margareta
Schneider, Dirk
Title: Covalently linking oligomerization-impaired GlpF protomers does not completely re-establish wild-type channel activity
Online publication date: 15-Apr-2019
Year of first publication: 2019
Language: english
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.
DDC: 570 Biowissenschaften
570 Life sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 09 Chemie, Pharmazie u. Geowissensch.
Place: Mainz
URN: urn:nbn:de:hebis:77-publ-590311
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC BY
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Journal: International journal of molecular sciences
Pages or article number: Art. 927
Publisher: Molecular Diversity Preservation International
Publisher place: Basel
Issue date: 2019
ISSN: 1422-0067
Publisher URL:
Publisher DOI: 10.3390/ijms20040927
Appears in collections:JGU-Publikationen

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