BIOCHEMICAL-CHARACTERIZATION OF A 34 KDA RIBONUCLEOPROTEIN (P34) PURIFIED FROM THE SPINACH CHLOROPLAST FRACTION AS AN EFFECTIVE PHOSPHATE ACCEPTOR FOR CASEIN KINASE-II
BIOCHEMICAL-CHARACTERIZATION OF A 34 KDA RIBONUCLEOPROTEIN (P34) PURIFIED FROM THE SPINACH CHLOROPLAST FRACTION AS AN EFFECTIVE PHOSPHATE ACCEPTOR FOR CASEIN KINASE-II
复制标题
DOI：
10.1016/0014-5793(93)80724-9
复制
发表时间：
1993-12-06
期刊：
影响因子：
3.5
通讯作者：
OHTSUKI, K
中科院分区：
文献类型：
--
作者：
KANEKATSU, M;MUNAKATA, H;OHTSUKI, K
从菠菜叶绿体的 1.0 M KCl 提取物中纯化出同质的 34 kDa 核糖核蛋白 (p34)，并被鉴定为酪蛋白激酶 II (CK-II) 的有效磷酸盐受体。 p34 的 N 端 21 个残基 (W-V-A-Q-T-S-E-E-E-Q-E-G-S-T-N-A-V-L-E-G-E) 与报道的 28RNP（叶绿体中质体 mRNA 3' 末端加工因子）的序列有 95% 相同。此外，DNA和RNA在体外显着刺激CK-II催化的p34磷酸化并诱导其构象变化，这表明叶绿体转录后调节中p34结合的RNA或DNA的生理活性受到CK-II特异性p34磷酸化的控制。
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.