Structure and Regulation Mechanism of Bacillus stearothermophilus dnaB-dnaG Complex

Abstract

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

Lu Ting . Structure and Regulation Mechanism of Bacillus stearothermophilus dnaB-dnaG Complex[J]. Biotechnology Bulletin, 2013, 0(6): 39-45.

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