Distinctive expression of a zinc-binding protein in rice callus grown in medium with high zinc concentration

We investigated the growth, contents of water-soluble protein and free amino acids of the callus of japonica rice (Oryza sativa L. cv. Nipponbare) cultured in liquid N6 medium containing a high concentration of zinc. Furthermore, we determined the N-terminal amino acid sequence of a Zn-binding prote...

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Bibliographic Details
Published in:Soil science and plant nutrition (Tokyo) 2000-03, Vol.46 (1), p.209-216
Main Authors: Saeki, Y. (Miyazaki Univ. (Japan). Faculty of Agriculture), Yasukouchi, A, Nagatomo, Y, Takaki, H
Format: Article
Language:English
Subjects:
Absorption. Translocation of ions and substances. Permeability
Agronomy. Soil science and plant productions
Biological and medical sciences
Biotechnology
CAL
CALLO
CALLUS
CINC
CULTURE MEDIA
Economic plant physiology
Fundamental and applied biological sciences. Psychology
In vitro culture
MEDIO DE CULTIVO
Metabolism
Metabolism. Physicochemical requirements
metallothionein-like protein
MILIEU DE CULTURE
N6 medium
Nutrition. Photosynthesis. Respiration. Metabolism
ORYZA SATIVA
Oryza sativa L
Plant physiology and development
PROTEINAS
PROTEINE
PROTEINS
rice callus
Tissue cultures, protoplasts
ZINC
zinc-binding protein
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Summary:We investigated the growth, contents of water-soluble protein and free amino acids of the callus of japonica rice (Oryza sativa L. cv. Nipponbare) cultured in liquid N6 medium containing a high concentration of zinc. Furthermore, we determined the N-terminal amino acid sequence of a Zn-binding protein expressed in large quantities in the callus. The addition of Zn stimulated the growth of the callus and increased the Zn concentration. The callus subjected to the high-Zn treatment (hereafter referred to as CHZn) contained a larger amount of soluble proteins and a smaller amount of free amino acids than the control callus. Zinc-binding proteins were separated by affinity chromatography. The SDS-PAGE pattern of these proteins showed a distinctive protein band of about 29 kDa. Especially, CHZn contained larger quantities of 29 kDa protein than the control callus. Twenty-seven N-terminal amino acids of the protein were sequenced as DYAPMTLTIVNNCPYPVWPGIQANSGH. Results of homology search to the amino acid sequences from the nr-aa database and the dbEST database suggested that this 29 kDa protein may be a novel zinc-binding protein and that the protein may regulate the concentration of free zinc in the cytoplasm of callus cells through its binding to zinc ions
ISSN:0038-0768
1747-0765
DOI:10.1080/00380768.2000.10408776