期刊
CELL REPORTS
卷 32, 期 3, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.celrep.2020.107928
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资金
- Royal Society University Research Fellowship [UF140053]
- BBSRC [BB/P018165/1, BBS/E/J/000PR9791]
- Royal Society [RG150448]
- EPSRC [EP/N027639/1, EP/R029407/1]
- Cambridge Tier-2 system (EPSRC Tier-2 capital grant) [EP/P020259/1]
- European Community's Seventh Framework Program (FP7/2007-2013) [283570]
- BBSRC [BB/P018165/1, BBS/E/J/000PR9791] Funding Source: UKRI
- EPSRC [EP/N027639/1] Funding Source: UKRI
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.
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