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Ultra Fast Mas Solid-State Nmr Studies Of Protein-Protein Interactions In The Bacterial Replisome, M Felletti, S Jehle, Y Wang, Kiyoshi Ozawa, S Jergic, G Otting, L Emsley, A Lesage, N Dixon, G Pintacuda
Ultra Fast Mas Solid-State Nmr Studies Of Protein-Protein Interactions In The Bacterial Replisome, M Felletti, S Jehle, Y Wang, Kiyoshi Ozawa, S Jergic, G Otting, L Emsley, A Lesage, N Dixon, G Pintacuda
Professor Nick E Dixon
Replication of genomic DNA in bacteria involves multiple stable and transient interactions among protein subunits constituting the replisome. Here we show how ultra-fast magic angle spinning (MAS) solid-state NMR (ssNMR) and 1H-detection on either deutereted or fully protonated samples, can give new information about protein-protein interactions in the E. coli replisome. We focused on two fundamental interactions: the first one between the C-terminal domain of the single-stranded (ss) DNA binding protein and its own DNA-binding site, and the second one between the DNA polymerase III subunits a and s. SSB (a tetramer of 79 kDa) has a structurally well-defined ssDNA …