生物技术通报 ›› 2013, Vol. 0 ›› Issue (6): 39-45.

• 综述与专论 • 上一篇    下一篇

嗜热脂肪芽孢杆菌dnaB-dnaG复合体的结构及调控机制

卢汀   

  1. (中国科学院成都生物所, 成都 610041)
  • 收稿日期:2013-06-20 修回日期:2013-06-20 出版日期:2013-06-20 发布日期:2013-06-20

Structure and Regulation Mechanism of Bacillus stearothermophilus dnaB-dnaG Complex

Lu Ting   

  1. (Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu 610041)
  • Received:2013-06-20 Revised:2013-06-20 Published:2013-06-20 Online:2013-06-20

摘要: 在嗜热脂肪芽孢杆菌(Bacillus stearothermophilus) 中, 解旋酶dnaB和引物酶dnaG组成的引发体在复制叉处解旋双链DNA, 并且对于合成冈崎片段(Okazaki fragment) 极其重要。 引物酶dnaG(P16) 的C末端的一个解旋酶相互作用结构域从结构和功能上调控这个相互作用。解旋酶dnaB的N末端和C末端的9个氨基酸残基及其连接区会影响dnaB和dnaG的相互作用。从蛋白质结构域和功能等方面阐述嗜热脂肪芽孢杆菌dnaB-dnaG复合物调控机理和研究进展。

关键词: 引物酶, 解旋酶, 复制叉, 复合体, 调控机制

Abstract: In Bacillus stearothermophilus, helicase dnaB and primase dnaG form primosomes to unwind duplex DNA at the replication folk, and it’s important for the synthesis of Okazaki fragments. A helicase-interacting domain at the C-terminal of primase dnaG(P16)can regulate the interaction structurally and functionally. 9 amino acid residues as well as their linker regions at the N-terminal and C-terminal of helicase dnaB can affect the interaction between dnaG and dnaB. Here we summarize the regulation mechanism of dnaB-dnaG complex from the protein domain and functional aspect and the recent progresses.

Key words: Primase, Helicase, Replication fork, Complex, Regulation mechanism