5'-二磷酸鸟苷-3'-二磷酸的体外降解
In vitro degradation of guanosine 5'-diphosphate, 3'-diphosphate.
作者信息
Sy J
出版信息
Proc Natl Acad Sci U S A. 1977 Dec;74(12):5529-33. doi: 10.1073/pnas.74.12.5529.
Abstract
The degradation of guanosine 5'-diphosphate,3'-diphosphate (ppGpp) by the "crude" ribosomal fraction of Escherichia coli CP78 (rel+, spoT+) was demonstrated and characterized. When the 3'-pyrophosphoryl group of ppGpp was hydrolyzed, the primary degradation product was 5'-GDP. Phosphorylation of ppGpp to guanosine 5'-triphosphate,3'-diphosphate (pppGpp) prior to degradation was not necessary. The degradation process required Mn2+ and was inhibited by EDTA. Levallorphan, an inhibitor of in vivo ppGpp degradation, also inhibited ppGpp degradation by the crude ribosome. Thiostrepton and tetracycline did not have any inhibitory effect, indicating that the reaction is not a reversal of pyrophosphorylation catalyzed by the stringent factor/ribosome complex. Crude ribosome fractions from E. coli NF161 and NF162, both spoT-, contained little degrading activity, but similar fractions of E. coli CP79, a relA- and spoT+ strain, contained ppGpp degrading activity.
摘要
已证实并表征了大肠杆菌CP78（rel +，spoT +）的“粗”核糖体部分对鸟苷5'-二磷酸3'-二磷酸（ppGpp）的降解作用。当ppGpp的3'-焦磷酸基团被水解时，主要降解产物是5'-GDP。降解前将ppGpp磷酸化为鸟苷5'-三磷酸3'-二磷酸（pppGpp）并非必需。降解过程需要Mn2 +，并受EDTA抑制。体内ppGpp降解的抑制剂左洛啡烷也抑制粗核糖体对ppGpp的降解。硫链丝菌素和四环素没有任何抑制作用，这表明该反应不是严紧因子/核糖体复合物催化的焦磷酸化的逆转。来自大肠杆菌NF161和NF162（均为spoT -）的粗核糖体部分几乎没有降解活性，但大肠杆菌CP79（relA -和spoT +菌株）的类似部分含有ppGpp降解活性。
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