Autoren:	Klein, Noreen Trefz, Margareta Schneider, Dirk
Titel:	Covalently linking oligomerization-impaired GlpF protomers does not completely re-establish wild-type channel activity
Online-Publikationsdatum:	15-Apr-2019
Erscheinungsdatum:	2019
Sprache des Dokuments:	Englisch
Zusammenfassung/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-Sachgruppe:	570 Biowissenschaften 570 Life sciences
Veröffentlichende Institution:	Johannes Gutenberg-Universität Mainz
Organisationseinheit:	FB 09 Chemie, Pharmazie u. Geowissensch.
Veröffentlichungsort:	Mainz
ROR:	https://ror.org/023b0x485
DOI:	http://doi.org/10.25358/openscience-769
URN:	urn:nbn:de:hebis:77-publ-590311
Version:	Published version
Publikationstyp:	Zeitschriftenaufsatz
Nutzungsrechte:	CC BY
Informationen zu den Nutzungsrechten:	https://creativecommons.org/licenses/by/4.0/
Zeitschrift:	International journal of molecular sciences 20 4
Seitenzahl oder Artikelnummer:	Art. 927
Verlag:	Molecular Diversity Preservation International
Verlagsort:	Basel
Erscheinungsdatum:	2019
ISSN:	1422-0067
URL der Originalveröffentlichung:	http://dx.doi.org/10.3390/ijms20040927
DOI der Originalveröffentlichung:	10.3390/ijms20040927
Enthalten in den Sammlungen:	JGU-Publikationen