Solution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit.

ABSTRACT: The solution structure of the C-terminal Domain V of the tau subunit of E. coli DNA polymerase III was determined by nuclear magnetic resonance (NMR) spectroscopy. The fold is unique to tau subunits. Amino acid sequence conservation is pronounced for hydrophobic residues that form the structural core of the protein, indicating that the fold is representative for tau subunits from a wide range of different bacteria. The interaction between the polymerase subunits tau and alpha was studied by NMR experiments where alpha was incubated with full-length C-terminal domain (tau(C)16), and domains shortened at the C-terminus by 11 and 18 residues, respectively. The only interacting residues were found in the C-terminal 30-residue segment of tau, most of which is structurally disordered in free tau

SUBMITTER: Su XC 

PROVIDER: S-EPMC1888800 | biostudies-literature | 2007

REPOSITORIES: biostudies-literature