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Cloning and characterization of the gene for a phloem‐specific glutathione S ‐transferase from rice leaves
Author(s) -
Fukuda Akari,
Okada Yoshihisa,
Suzui Nobuo,
Fujiwara Toru,
Yoneyama Tadakatsu,
Hayashi Hiroaki
Publication year - 2004
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.0031-9317.2004.0253.x
Subject(s) - phloem , glutathione s transferase , glutathione , biology , sieve tube element , cloning (programming) , molecular cloning , biochemistry , molecular mass , amino acid , peptide sequence , escherichia coli , gene , sequence analysis , clone (java method) , oryza sativa , botany , enzyme , computer science , programming language
The N‐terminal amino‐acid sequence was determined for a major r ice p hloem p rotein with a molecular mass of 31 kDa, named RPP31. The corresponding full‐length rice EST‐clone was cloned based on the amino acid sequence. The predicted total amino‐acid sequence of RPP31 shared high similarity with plant glutathione S ‐transferases (GSTs). Recombinant RPP31 produced in Escherichia coli and rice phloem sap showed GST activity. Immunocytological analysis indicated that RPP31 is localized in the phloem region of leaves. In mature leaves, the signal was restricted to sieve element–companion cell complexes, and was stronger in sieve elements than in companion cells. Although some plant GSTs are known to be induced by xenobiotics, the amount of RPP31 was not affected by treatments with an herbicide, pretilachlor, and/or its safener, fenclorim. These results suggest that RPP31 is an active GST restricted to the phloem region of normal rice leaves.