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The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere

AutorFisher, Gemma LM; Pastrana, César L.; Higman, Victoria A.; Koh, Alan; Taylor, James A.; Butterer, Annika; Craggs, Timothy; Sobott, Frank; Murray, Heath; Crump, Matthew P.; Moreno-Herrero, Fernando; Dillingham, Mark S.
Palabras claveB. subtilis
NMR
Spo0J
bacterial centromere
biophysics
chromosome segregation
chromosomes
genes
single-molecule
structural biology
Fecha de publicación15-dic-2017
EditoreLife Sciences Publications
CitacióneLife 6: e28086 (2017)
ResumenThe ParB protein forms DNA bridging interactions around parS to condense DNA and earmark the bacterial chromosome for segregation. The molecular mechanism underlying the formation of these ParB networks is unclear. We show here that while the central DNA binding domain is essential for anchoring at parS, this interaction is not required for DNA condensation. Structural analysis of the C-terminal domain reveals a dimer with a lysine-rich surface that binds DNA non-specifically and is essential for DNA condensation in vitro. Mutation of either the dimerisation or the DNA binding interface eliminates ParB-GFP foci formation in vivo. Moreover, the free C-terminal domain can rapidly decondense ParB networks independently of its ability to bind DNA. Our work reveals a dual role for the C-terminal domain of ParB as both a DNA binding and bridging interface, and highlights the dynamic nature of ParB networks in Bacillus subtilis.
Versión del editorhttp://dx.doi.org/10.7554/eLife.28086
URIhttp://hdl.handle.net/10261/160250
DOI10.7554/eLife.28086.
E-ISSN2050-084X
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