Biochemical characterization of a 34 kda ribonucleoprotein (p34) purified from the spinach chloroplast fraction as an effective phosphate acceptor for casein kinase II

FEBS Letters

Ohtsuki, Kenzo³  Munakata, Hiroshi¹  Furuzono, Kazuhisa³  Kanekatsu, Motoki² 

[1] 2nd Department of Biochemistry, Tohoku University School of Medicine, Sendai 980, Japan;Laboratory of Biology, School of Liberal Arts and Sciences, Kitasato University, Kitasato 1-15-1, Sagamihara 228, Japan;Laboratory of Genetical Biochemistry, Department of Bioscience, Kitasato University School of Hygienic Science, Sagamihara 228, Japan

关键词: Ribonucleoprotein;    Casein kinase II;    Protein phosphorylation;    Plastid mRNA 3' end processing;    Chloroplast;    Spinach;    p34;    34 kDa ribonucleoprotein;    CK-II;    casein kinaseII;    28RNP;    28 kDa ribonucleoprotein;    dsDNA;    double-stranded DNA;    ssDNA;    single-stranded DNA;    SDS-PAGE;    sodium do-decylsulfate-polyacrylamide gel electrophoresis;    DTT;    dithiothreitol;    2-ME;    2-mercaptoethanol;    PMSF;    phenylmethylsulfonyl fluoride;    HPLC;    high performance liquid chromatography;    CD;    circular dichroism;   

DOI  :  10.1016/0014-5793(93)80724-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown