In vivo activation of recombinant cAPK catalytic subunit active site mutants by coexpression of the wild‐type enzyme, evidence for intermolecular cotranslational phosphorylation
In vivo activation of recombinant cAPK catalytic subunit active site mutants by coexpression of the wild‐type enzyme, evidence for intermolecular cotranslational phosphorylation
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通过野生型酶的共表达体内激活重组cAPK催化亚基活性位点突变体，分子间共翻译磷酸化的证据
DOI：
10.1016/0014-5793(96)00717-x
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发表时间：
1996
期刊：
影响因子：
3.5
通讯作者：
D. Bossemeyer
中科院分区：
文献类型：
--
作者：
A. Girod;V. Kinzel;D. Bossemeyer
The catalytic subunit of cAMP dependent protein kinase (cAPK) carries two stable autophosphorylated residues. One of them, Thr197, residues in the so‐called protein kinase activation segment, and needs to be phosphorylated for full activity and protein kinase inhibitor binding of the enzyme. While wild‐type recombinant mammalian C‐subunit, expressed inE. coli, can fully autoactivate itself by phosphorylation at Thr197, many active site mutants lack this autophosphorylation activity, so that the primary effects of the mutations become obscured. Two active site mutants of bovine C‐subunit, defective in protein kinase inhibitor peptide binding, were activated by wild‐type enzyme in vivo, but could not be activated in vitro, demonstrating intermolecular and presumably cotranslational autophosphorylation. The results may delineate strategies for the expression and mutagenesis of other protein kinases with requirements for activation segment phosphorylation.
影响因子：
2.9
作者：
ADAMS, JA;MCGLONE, ML;TAYLOR, SS
通讯作者：
TAYLOR, SS
cAMP 依赖性蛋白激酶催化亚基的 C α 和 C β 亚型的亲和纯化。
DOI：
--
发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Olsen,SR;Uhler,MD
通讯作者：
Uhler,MD
影响因子：
56.9
作者：
KNIGHTON, DR;ZHENG, JH;SOWADSKI, JM
通讯作者：
SOWADSKI, JM