Integrative modelling coupled with ion mobility mass spectrometry reveals structural features of the clamp loader in complex with single-stranded DNA binding protein.

Journal article

DNA polymerase III, a decameric 420-kDa assembly, simultaneously replicates both strands of the chromosome in Escherichia coli. A subassembly of this holoenzyme, the seven-subunit clamp loader complex, is responsible for loading the sliding clamp (β2) onto DNA. Here, we use structural information derived from ion mobility mass spectrometry (IM-MS) to build three-dimensional models of one form of the full clamp loader complex, γ3δδ'ψχ (254 kDa). By probing the interaction between the clamp loa...

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Authors: Politis, A; Park, A; Hall, Z; Ruotolo, B; Robinson, C

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 425
• Issue: 23
• Pages: 4790-4801
• Publication date: 2013-11-01
• DOI: 10.1016/j.jmb.2013.04.006
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Escherichia coli; DNA-Binding Proteins; DNA Polymerase III; Models, Molecular; Imaging, Three-Dimensional; Mass Spectrometry; Multienzyme Complexes; DNA, Single-Stranded