Suppr超能文献

噬菌体Mu转座酶的化学计量使用

Stoichiometric use of the transposase of bacteriophage Mu.

作者信息

Pato M L, Reich C

出版信息

Cell. 1984 Jan;36(1):197-202. doi: 10.1016/0092-8674(84)90089-8.

Abstract

The transposase of bacteriophage Mu (gene A protein) mediates the coupled replication and integration processes that constitute transposition during the lytic cycle. Our previous results showed that the activity of the A protein is unstable, as its continued synthesis is required to maintain Mu DNA replication throughout the lytic cycle. We present here the results of experiments in which the A protein is used stoichiometrically and must be synthesized de novo for each round of Mu DNA replication. Induction of a Mu lysogen in the absence of DNA replication allows accumulation of potential for a single round of Mu DNA replication. Once achieved, this potential is stable even in the absence of further protein synthesis. Release of inhibition of DNA replication leads to a single semi-conservative replicative transposition event, followed by later rounds only if additional synthesis of the A protein is allowed.

摘要

噬菌体Mu的转座酶(基因A蛋白)介导了在裂解周期中构成转座的耦合复制和整合过程。我们之前的结果表明,A蛋白的活性不稳定,因为在整个裂解周期中需要持续合成该蛋白以维持Mu DNA复制。我们在此展示了一些实验结果,其中A蛋白以化学计量方式使用,并且每一轮Mu DNA复制都必须重新合成。在无DNA复制的情况下诱导Mu溶原菌可积累进行一轮Mu DNA复制的潜力。一旦实现,即使在没有进一步蛋白质合成的情况下,这种潜力也是稳定的。解除对DNA复制的抑制会导致一次半保留复制性转座事件,只有在允许额外合成A蛋白的情况下,随后才会进行后续轮次的转座。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验