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Plant and Cell Physiology, 1995, Vol. 36, No. 8 1649-1656
© 1995

Chloroplast Ribonucleoproteins (RNPs) as Phosphate Acceptors for Casein Kinase II: Purification by ssDNA-Cellulose Column Chromatography

Motoki Kanekatsu1, Akiyoshi Ezumi2, Takahiro Nakamura2 and Kenzo Ohtsuki2

1 Laboratory of Biology, School of Liberal Arts and Sciences, Kitasato University Sagamihara, 228 Japan
2 Department of Bioscience, School of Hygienic Sciences, Kitasato University Sagamihara, 228 Japan

Using ssDNA-cellulose column chromatography, a 34 kDa ribonucleoprotein (p34) has been purified from a 0.4 M KCl crude extract of spinach chloroplasts as an effective phosphate acceptor for casein kinase II (CK-II) in vitro. Monomeric and oligomeric CK-IIs were copurified with p34 by the column chromatography and the kinases were separated from p34 by means of Mono Q column chromatography. It was found that (i) the purified p34 (pi 4.9) was phosphorylated specifically by CK-II in vitro; and (ii) similar polypeptides, such as p35 (pI 4.7) and p39 (pI 4.9) in maize and p33 (pI 4.7) in liverwort, were detected as ssDNA-binding chloroplast proteins phosphorylated by CK-II in vitro. The findings suggest that (i) RNPs that function as phosphate acceptors for CK-II exist commonly in chloroplasts among plant cells; and (ii) the physiological activity of RNPs is regulated by their specific phosphorylation by CK-II in chloroplasts.

(Received July 3, 1995; Accepted October 5, 1995)
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