Complexed Crystal Structure of Replication Restart Primosome Protein Prib Reveals a Novel Single-stranded Dna-binding Mode.
From: Institute of Molecular Biology, Academia Sinica, Taipei, 115, Taiwan.
Nucleic acids research
- Publish Date: 2006
- ISSN: 1362-4962
- Volume: 34
- Issue: 14
- Pages: 3878-86
- Medium: Internet
- Language: English
- Citation (JAMA): Huang Cheng-Yang, Hsu Che-Hsiung, Sun Yuh-Ju, et al. Complexed Crystal Structure of Replication Restart Primosome Protein Prib Reveals a Novel Single-stranded Dna-binding Mode.. Nucleic Acids Res. 2006;34:3878-86
Abstract
PriB is a primosomal protein required for replication restart in Escherichia coli. PriB stimulates PriA helicase activity via interaction with single-stranded DNA (ssDNA), but the molecular details of this interaction remain unclear. Here, we report the crystal structure of PriB complexed with a 15 bases oligonucleotide (dT15) at 2.7 A resolution. PriB shares structural similarity with the E.coli ssDNA-binding protein (EcoSSB). However, the structure of the PriB-dT15 complex reveals that PriB binds ssDNA differently. Results from filter-binding assays show that PriB-ssDNA interaction is salt-sensitive and cooperative. Mutational analysis suggests that the loop L45 plays an important role in ssDNA binding. Based on the crystal structure and biochemical analyses, we propose a cooperative mechanism for the binding of PriB to ssDNA and a model for the assembly of the PriA-PriB-ssDNA complex. This report presents the first structure of a replication restart primosomal protein complexed with DNA, and a novel model that explains the interactions between a dimeric oligonucleotide-binding-fold protein and ssDNA.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, DNA, Circular, DNA, Single-Stranded, DNA-Binding Proteins, Dimerization, Escherichia coli Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Oligonucleotides, Protein Binding, Sequence Alignment
Check for Full Text / PubMed Unique Identifier (PMID): 16899446
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