5NOC

Solution NMR Structure of the C-terminal domain of ParB (Spo0J)

Summary for 5NOC

• Entry DOI: 10.2210/pdb5noc/pdb
• NMR Information: BMRB: 34122
• Descriptor: Stage 0 sporulation protein J (1 entity in total)
• Functional Keywords: homodimer, dna binding protein, bacterial, chromosome, segregation, centromere
• Biological source: Bacillus subtilis subsp. subtilis str. 168
• Total number of polymer chains: 2
• Total formula weight: 16222.40

Authors

Higman, V.A.,Fisher, G.L.M.,Dillingham, M.S.,Crump, M.P. (deposition date: 2017-04-11, release date: 2017-12-13, Last modification date: 2024-06-19)

Primary citation

Fisher, G.L.,Pastrana, C.L.,Higman, V.A.,Koh, A.,Taylor, J.A.,Butterer, A.,Craggs, T.,Sobott, F.,Murray, H.,Crump, M.P.,Moreno-Herrero, F.,Dillingham, M.S.
The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere.
Elife, 6:-, 2017

PubMed Abstract: The ParB protein forms DNA bridging interactions around 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 , 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 .

PubMed: 29244022
DOI: 10.7554/eLife.28086

Experimental method

SOLUTION NMR