Grassl, Renate and Robl, Ingrid and Opekarova, Miroslava and Tanner, Widmar (2000) 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. FEBS LETTERS, 468 (2-3). pp. 225-230. ISSN 0014-5793, 1873-3468
Full text not available from this repository. (Request a copy)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. (C) 2000 Federation of European Biochemical Societies.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MEMBRANE H+-ATPASE; SCHIZOSACCHAROMYCES-POMBE; HETEROLOGOUS EXPRESSION; GLUCOSE-TRANSPORTER; COTRANSPORTER; CLONING; YEAST; PROTEINS; MUTANTS; CARRIER; sugar transport; HUP1; C-terminus structure; tryptic digestion; monoclonal antibody; Chlorella kessleri |
| Subjects: | 500 Science > 580 Botanical sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften > Lehrstuhl für Zellbiologie und Pflanzenphysiologie (Prof. Dr. Klaus Grasser) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Jun 2022 06:12 |
| Last Modified: | 07 Jun 2022 06:12 |
| URI: | https://pred.uni-regensburg.de/id/eprint/42816 |
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