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Plant and Cell Physiology, 1995, Vol. 36, No. 3 505-510
© 1995

Molecular Cloning and Characterization of cDNA for a Rice Protein that Contains Seven Repetitive Segments of the Trp-Asp Forty-Amino-Acid Repeat (WD-40 Repeat)

Yukimoto Iwasaki1,3, Masayasu Komano1, Atsushi Ishikawa1, Takuji Sasaki2 and Tadashi Asahi1

1Department of Bioscience, Faculty of Biotechnology, Fukui Prefectural University Kenjojima, Matsuoka-cho, Yoshida-gun, Fukui, 910-11 Japan
2Rice Genome Research Program, National Institute of Agrobiological Resources Kannondai, Tsukuba, Ibaraki, 305 Japan

3To whom correspondence should be addressed.

A cDNA clone for a polypeptide that contained seven repetitive segments of the Trp-Asp forty-amino-acid repeat (WD-40 repeat) was isolated from a cDNA library prepared from the greening leaves of rice. The cDNA was 1,285 bp long and contained an open reading frame that encoded a protein of 334 amino acid residues, which was designated it RWD (rice protein containing the WD-40 repeat). RWD exhibited greater homology to a group of receptor for activated C-kinase (RACK), a product of auxin-regulated gene from cultured cells (arcA) and a Chlamydomonas ß subunit-like polypeptide (Cblp) rather than to the ß subunits of heterotrimeric G protein complexes. The mRNA for RWD (1.3 kb) was found in all organs of rice plants, in particular, in roots. Therefore, RWD is suggested to be a protein that is expressed constitutively.

(Received September 27, 1994; Accepted February 8, 1995)
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