Cytosolic double-stranded RNA-dependent protein kinase is likely a dimer of partially phosphorylated Mr = 66,000 subunits.
Cytosolic double-stranded RNA-dependent protein kinase is likely a dimer of partially phosphorylated Mr = 66,000 subunits.
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DOI：
10.1016/s0021-9258(19)50079-5
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发表时间：
1992-05
期刊：
影响因子：
--
通讯作者：
J. Langland;Bertram L. Jacobs
中科院分区：
文献类型：
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作者：
J. Langland;Bertram L. Jacobs
本报告中描述的工作表明存在两种生物化学上可区分的干扰素诱导型双链RNA依赖性蛋白激酶。从干扰素处理细胞的胞质组分（S-100）和核糖体盐洗涤组分中分离的激酶在其色谱性质上不同。S-100激酶以M（r）= 140，000 - 160，000从凝胶过滤柱洗脱，并且主要是阴离子性质，而核糖体激酶以M（r）= 66，000洗脱，并且主要是阳离子性质。S-100激酶的纯化制剂含有M（r）= 66，000亚基P1，作为唯一以化学计量量存在的多肽，因此S-100激酶似乎是P1亚基的二聚体。S-100激酶的二聚化依赖于酶的磷酸化状态。从S-100分离的激酶被部分磷酸化。通过用碱性磷酸酶处理S-100激酶的去磷酸化导致酶的单体形式，其生化特征类似于核糖体盐洗激酶。
The work described in this report suggests the existence of two biochemically distinguishable forms of the interferon-inducible, double-stranded RNA-dependent protein kinase. Kinase isolated from the cytosolic fraction (S-100) and the ribosome salt wash fraction of interferon-treated cells differed in their chromatographic properties. S-100 kinase eluted from a gel filtration column with M(r) = 140,000-160,000 and was predominantly anionic in nature, whereas ribosomal kinase eluted with M(r) = 66,000 and was predominantly cationic in nature. Purified preparations of S-100 kinase contained the M(r) = 66,000 subunit, P1, as the only polypeptide present in stoichiometric amounts, and thus the S-100 kinase appears to be a dimer of P1 subunits. Dimerization of the S-100 kinase was dependent on the phosphorylation state of the enzyme. Kinase isolated from S-100 was partially phosphorylated. Dephosphorylation of the S-100 kinase by treatment with alkaline phosphatase resulted in a monomeric form of the enzyme with biochemical characteristics similar to that of the ribosome salt wash kinase.