期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 14, 页码 9470-9483出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku633
关键词
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资金
- Chinese Ministry of Science and Technology [2012CB917200]
- Chinese National Natural Science Foundation [31130018, 31370732, 31270014, 30900224]
- Science and Technological Fund of Anhui Province for Outstanding Youth [1308085JGD08]
DnaT is a primosomal protein that is required for the stalled replication fork restart in Escherichia coli. As an adapter, DnaT mediates the PriA-PriB-ssDNA ternary complex and the DnaB/C complex. However, the fundamental function of DnaT during PriA-dependent primosome assembly is still a black box. Here, we report the 2.83 angstrom DnaT(84-153)-dT10 ssDNA complex structure, which reveals a novel three-helix bundle single-stranded DNA binding mode. Based on binding assays and negative-staining electron microscopy results, we found that DnaT can bind to phiX 174 ssDNA to form nucleoprotein filaments for the first time, which indicates that DnaT might function as a scaffold protein during the PriA-dependent primosome assembly. In combination with biochemical analysis, we propose a cooperative mechanism for the binding of DnaT to ssDNA and a possible model for the assembly of PriA-PriB-ssDNA-DnaT complex that sheds light on the function of DnaT during the primosome assembly and stalled replication fork restart. This report presents the first structure of the DnaT C-terminal complex with ssDNA and a novel model that explains the interactions between the three-helix bundle and ssDNA.
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