被噬菌体T7激酶Gp0.7磷酸化的大肠杆菌RNA聚合酶β'亚基残基的定位
Localization of the Escherichia coli RNA polymerase beta' subunit residue phosphorylated by bacteriophage T7 kinase Gp0.7.
作者信息
Severinova Elena, Severinov Konstantin
机构信息
Waksman Institute, Piscataway, NJ 08854, USA.
出版信息
J Bacteriol. 2006 May;188(10):3470-6. doi: 10.1128/JB.188.10.3470-3476.2006.
Abstract
During bacteriophage T7 infection, the Escherichia coli RNA polymerase beta' subunit is phosphorylated by the phage-encoded kinase Gp0.7. Here, we used proteolytic degradation and mutational analysis to localize the phosphorylation site to a single amino acid, Thr(1068), in the evolutionarily hypervariable segment of beta'. Using a phosphomimetic substitution of Thr(1068), we show that phosphorylation of beta' leads to increased rho-dependent transcription termination, which may help to switch from host to viral RNA polymerase transcription during phage development.
摘要
在噬菌体T7感染过程中，大肠杆菌RNA聚合酶β'亚基被噬菌体编码的激酶Gp0.7磷酸化。在此，我们利用蛋白水解降解和突变分析将磷酸化位点定位到β'进化上高度可变区段中的单个氨基酸Thr(1068)。通过对Thr(1068)进行拟磷酸化取代，我们发现β'的磷酸化导致rho依赖性转录终止增加，这可能有助于在噬菌体发育过程中从宿主RNA聚合酶转录转换为病毒RNA聚合酶转录。
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