A repeating 11‐mer amino acid motif and plant desiccation

Summary Among the proteins that accumulate as plant seeds desiccate are several protein families that are composed principally of a tandemly repeated 11‐mer amino acid motif. Proteins containing the same motif accumulate in the desiccating leaves of a desiccation‐tolerant plant species. This motif i...

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Bibliographic Details
Published in:The Plant journal : for cell and molecular biology 1993-03, Vol.3 (3), p.363-369
Main Author: Dure, Leon
Format: Article
Language:English
Subjects:
Adaptation, Physiological
Amino Acid Sequence
Brassica napus
Heat-Shock Proteins - genetics
Hordeum vulgare
Molecular Sequence Data
Plant Proteins - genetics
Plant Proteins - metabolism
Plants - genetics
Plants - metabolism
Repetitive Sequences, Nucleic Acid
Sequence Homology, Amino Acid
Water - metabolism
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Summary:Summary Among the proteins that accumulate as plant seeds desiccate are several protein families that are composed principally of a tandemly repeated 11‐mer amino acid motif. Proteins containing the same motif accumulate in the desiccating leaves of a desiccation‐tolerant plant species. This motif is characterized by apolar residues in positions 1, 2, 5 and 9, and charged or amide residues in positions 3, 6, 7, 8 and 11. An α helical arrangement of the 11‐mer repeating unit gives an amphiphilic helix whose hydrophobic stripe twists in a right‐handed fashion around the helix. Should these proteins dimerize via binding of their hydrophobic faces, a right‐handed coiled coil would be formed. Such a structure has not previously been observed. A conceivable function for these proteins in ion sequestration in the desiccated state is proposed.
ISSN:0960-7412
1365-313X
DOI:10.1046/j.1365-313X.1993.t01-19-00999.x