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Biochemical characterization of a 34 kda ribonucleoprotein (p34) purified from the spinach chloroplast fraction as an effective phosphate acceptor for casein kinase II
Author(s) -
Kanekatsu Motoki,
Munakata Hiroshi,
Furuzono Kazuhisa,
Ohtsuki Kenzo
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80724-9
Subject(s) - chloroplast , ribonucleoprotein , biochemistry , phosphorylation , spinach , rna , casein kinase 2 , kinase , biology , protein kinase a , casein kinase 1 , phosphate , microbiology and biotechnology , chemistry , cyclin dependent kinase 2 , gene
A 34 kDa ribonucleoprotein (p34) was purified to homogeneity from a 1.0 M KCl extract of spinach chloroplasts and characterized as an effective phosphate acceptor for casein kinase II (CK‐II). The N‐terminal 21 residues (W‐V‐A‐Q‐T‐S‐E‐E‐E‐Q‐E‐G‐S‐T‐N‐A‐V‐L‐E‐G‐E) of p34 were 95% identical with the sequence reported for 28RNP (plastid mRNA 3' end processing factor in chloroplast). Moreover, the findings that DNAs as well as RNAs significantly stimulate the CK‐II catalyzed phosphorylation of p34 in vitro and induce its conformational change, suggest that the physiological activity of p34‐bound RNA or DNA in chloroplast post‐transcriptional regulation is controlled by specific p34 phosphorylation by CK‐II.