@article{kojetin_mclaughlin_thompson_dubnau_prepiak_rance_cavanagh_2009, title={Structural and Motional Contributions of the Bacillus subtilis ClpC N-Domain to Adaptor Protein Interactions}, volume={387}, ISSN={["1089-8638"]}, DOI={10.1016/j.jmb.2009.01.046}, abstractNote={The AAA + (ATPases associated with a variety of cellular activities) superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. As part of a large oligomeric complex, ClpC controls an array of cellular processes by recognizing, unfolding, and providing misfolded and aggregated proteins as substrates for the ClpP peptidase. ClpC is unique compared to other HSP100/Clp proteins, as it requires an adaptor protein for all fundamental activities. The NMR solution structure of the N-terminal repeat domain of ClpC (N-ClpCR) comprises two structural repeats of a four-helix motif. NMR experiments used to map the MecA adaptor protein interaction surface of N-ClpCR reveal that regions involved in the interaction possess conformational flexibility and conformational exchange on the microsecond-to-millisecond timescale. The electrostatic surface of N-ClpCR differs substantially from the N-domain of Escherichia coli ClpA and ClpB, suggesting that the electrostatic surface characteristics of HSP100/Clp N-domains may play a role in adaptor protein and substrate interaction specificity, and perhaps contribute to the unique adaptor protein requirement of ClpC.}, number={3}, journal={JOURNAL OF MOLECULAR BIOLOGY}, author={Kojetin, Douglas J. and McLaughlin, Patrick D. and Thompson, Richele J. and Dubnau, David and Prepiak, Peter and Rance, Mark and Cavanagh, John}, year={2009}, month={Apr}, pages={639–652} }
 @article{kojetin_mclaughlin_thompson_venters_rance_cavanagh_2007, title={NMR assignment of the N-terminal repeat domain of Bacillus subtilis ClpC}, volume={1}, ISSN={["1874-2718"]}, DOI={10.1007/s12104-007-9046-8}, abstractNote={The HSP100/AAA+ superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. We present here the backbone and side-chain assignments of the N-terminal repeat domain (residues 1-145) of ClpC from Bacillus subtilis.}, number={2}, journal={BIOMOLECULAR NMR ASSIGNMENTS}, author={Kojetin, Douglas J. and McLaughlin, Patrick D. and Thompson, Richele J. and Venters, Ronald A. and Rance, Mark and Cavanagh, John}, year={2007}, month={Dec}, pages={163–165} }
 @article{mclaughlin_bobaya_regel_thompson_hoch_cavanagh_2007, title={Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition}, volume={581}, ISSN={["0014-5793"]}, DOI={10.1016/j.febslet.2007.02.061}, abstractNote={Several alanine mutations in the response regulator Spo0F induce hypersporulation in Bacillus subtilis. L66A, I90A and H101A mutants are purported to be involved in contacts stabilizing the orientation of the α4‐helix and hence the β4–α4 kinase recognition loop. Y13A is thought to affect the orientation of the α1‐helix and consequently phosphatase action. Using comparative NMR chemical shift analyses for these mutants, we have confirmed these suppositions and isolated residues in Spo0F critical in sensor kinases discrimination. In addition, we discuss how buried residues and intra‐protein communication networks contribute to precise molecular recognition by ensuring that the correct surface is presented.}, number={7}, journal={FEBS LETTERS}, author={McLaughlin, Patrick D. and Bobaya, Benjamm G. and Regel, Erin J. and Thompson, Richele J. and Hoch, James A. and Cavanagh, John}, year={2007}, month={Apr}, pages={1425–1429} }