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The C‐terminal tetrapeptide HWFW of the Chlorella HUP1 hexose/H + ‐symporter is essential for full activity and an α‐helical structure of the C‐terminus
Author(s) -
Graßl Renate,
Robl Ingrid,
Opekarovà Miroslava,
Tanner Widmar
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01230-8
Subject(s) - symporter , major facilitator superfamily , tetrapeptide , biochemistry , trypsin , chemistry , amino acid , hexose , epitope , peptide , stereochemistry , microbiology and biotechnology , biology , transporter , antibody , enzyme , gene , genetics
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 α‐helical conformation in contrast to the wild type C‐terminal peptide with an α‐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.