Functional characterization of a microbial aquaglyceroporin
| Autor: | Isabelle Pellerin, Alexandrine Froger, Patrick Bron, Christian Delamarche, Françoise Le Cahérec, Jean-François Hubert, Valérie Lagrée, Daniel Thomas, Jean-Paul Rolland, Stéphane Deschamps |
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| Rok vydání: | 2001 |
| Předmět: |
Glycerol
Glycerol transport Aquaporin In Vitro Techniques Biology Aquaporins medicine.disease_cause Microbiology Xenopus laevis Escherichia coli medicine Animals Membrane Glycoproteins Water transport Cryoelectron Microscopy Lactococcus lactis Major intrinsic proteins Water Biological Transport biology.organism_classification Aquaglyceroporins Biochemistry Porin Oocytes Sequence Alignment |
| Zdroj: | Microbiology. 147:1129-1135 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/00221287-147-5-1129 |
| Popis: | The major intrinsic proteins (MIPs) constitute a widespread membrane channel family essential for osmotic cell equilibrium. The MIPs can be classified into three functional subgroups: aquaporins, glycerol facilitators and aquaglyceroporins. Bacterial MIP genes have been identified in archaea as well as in Gram-positive and Gram-negative eubacteria. However, with the exception of Escherichia coli, most bacterial MIPs have been analysed by sequence homology. Since no MIP has yet been functionally characterized in Gram-positive bacteria, we have studied one of these members from Lactococcus lactis. This MIP is shown to be permeable to glycerol, like E. coli GlpF, and to water, like E. coli AqpZ. This is the first characterization of a microbial MIP that has a mixed function. This result provides important insights to reconstruct the evolutionary history of the MIP family and to elucidate the molecular pathway of water and other solutes in these channels. |
| Databáze: | OpenAIRE |
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