Chloroplast ribonucleoproteins (RNPs) as phosphate acceptors for casein kinase II: Purification by ssDNA-cellulose column chromatography

Motoki Kanekatsu, Akiyoshi Ezumi, Takahiro Nakamura, Kenzo Ohtsuki

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1649-1656
Number of pages8
JournalPlant and Cell Physiology
Volume36
Issue number8
Publication statusPublished - Dec 1 1995
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

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