The C-terminal tetrapeptide HWFW of the Chlorella HUP1 hexose/H(+)-symporter is essential for full activity and an alpha-helical structure of the C-terminus |
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Authors: | Grassl R Robl I Opekarovà M Tanner W |
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Institution: | Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universit?t Regensburg, Universit?tsstr. 31, 93040, Regensburg, Germany. renate.grassl@biologie.uni-regensburg.de |
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Abstract: | C-terminal tails of plant hexose/H(+)-symporters of the major facilitator superfamily contain a highly conserved motif of four amino acids: HWFW. A deletion of these four amino acids in the Chlorella HUP1 protein leads to a decrease in transport activity by a factor of 3-4. The mutated tail is highly sensitive to trypsin; it does not show alpha-helical conformation in contrast to the wild type C-terminal peptide with an alpha-helical content of at least 15%. The production of monoclonal antibody 416B8 recognizing an epitope within the central loop of HUP1 protein has been a prerequisite for the experiments described. |
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