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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Diversification of DNA-binding specificity by permissive and specificity-switching mutations in the ParB/Noc protein family Adam S. B. Jalal , Ngat T. Tran , Clare E. Stevenson , Elliot W. Chan , Rebecca Lo , Xiao Tan , Agnes Noy , David M. Lawson , Tung B. K. Le Cell Reports 32 DOI: 10.1016/j.celrep.2020.107928 Diamond Proposal Number(s): [18565] Open Access Show Abstract ▼ Abstract: Specific interactions between proteins and DNA are essential to many biological processes. Yet, it remains unclear how the diversification in DNA-binding specificity was brought about, and the mutational paths that led to changes in specificity are unknown. Using a pair of evolutionarily related DNA-binding proteins, each with a different DNA preference (ParB [Partitioning Protein B] and Noc [Nucleoid Occlusion Factor], which both play roles in bacterial chromosome maintenance), we show that specificity is encoded by a set of four residues at the protein-DNA interface. Combining X-ray crystallography and deep mutational scanning of the interface, we suggest that permissive mutations must be introduced before specificity-switching mutations to reprogram specificity and that mutational paths to new specificity do not necessarily involve dual-specificity intermediates. Overall, our results provide insight into the possible evolutionary history of ParB and Noc and, in a broader context, might be useful for understanding the evolution of other classes of DNA-binding proteins.	Jul 2020

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I03-Macromolecular Crystallography
I04-Macromolecular Crystallography

Diversification of DNA-binding specificity by permissive and specificity-switching mutations in the ParB/Noc protein family

Adam S. B. Jalal , Ngat T. Tran , Clare E. Stevenson , Elliot W. Chan , Rebecca Lo , Xiao Tan , Agnes Noy , David M. Lawson , Tung B. K. Le

Cell Reports 32

DOI: 10.1016/j.celrep.2020.107928

Diamond Proposal Number(s): [18565]