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ppGpp 抑制大肠杆菌 DnaG 引发酶的活性。

ppGpp inhibits the activity of Escherichia coli DnaG primase.

机构信息

Department of Molecular Biology, University of Gdańsk, Kładki 24, 80-822 Gdańsk, Poland.

出版信息

Plasmid. 2010 Jan;63(1):61-7. doi: 10.1016/j.plasmid.2009.11.002. Epub 2009 Nov 27.

Abstract

DNA primase is an enzyme required for replication of both chromosomes and vast majority of plasmids. Guanosine tetra- and penta-phosphate (ppGpp and pppGpp, respectively) are alarmones of the bacterial stringent response to starvation and stress conditions, and act by modulation of the RNA polymerase activity. Recent studies indicated that the primase-catalyzed reaction is also inhibited by (p)ppGpp in Bacillus subtilis, where a specific regulation of DNA replication elongation, the replication fork arrest, was discovered. Although in Escherichia coli such a replication regulation was not reported to date, here we show that E. coli DnaG primase is directly inhibited by ppGpp and pppGpp. However, contrary to the B. subtilis primase response to the stringent control alarmones, the E, coli DnaG was inhibited more efficiently by ppGpp than by pppGpp.

摘要

DNA 引物酶是一种酶,需要复制的染色体和绝大多数的质粒。鸟苷四 - 和五 - 磷酸(分别为 ppGpp 和 pppGpp)是细菌严格响应饥饿和压力条件的警报素,通过调节 RNA 聚合酶活性起作用。最近的研究表明,引物酶催化的反应也受到枯草芽孢杆菌中(p)ppGpp 的抑制,在那里发现了 DNA 复制延伸的特定调节,复制叉停滞。尽管到目前为止,尚未在大肠杆菌中报道这种复制调控,但我们在这里表明,大肠杆菌 DnaG 引物酶直接受到 ppGpp 和 pppGpp 的抑制。然而,与枯草芽孢杆菌引物酶对严格控制警报素的反应相反,大肠杆菌 DnaG 被 ppGpp 抑制的效率比 pppGpp 高。

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