ParB-type DNA Segregation Proteins Are CTP-Dependent Molecular Switches.

By Manuel Osorio-Valeriano, F. Altegoer, Wieland Steinchen, Svenja Urban, Y. Liu, G. Bange, M. Thanbichler. 2019

159 citations recorded by the source corpus.

During cell division, newly replicated DNA is actively segregated to the daughter cells. In most bacteria, this process involves the DNA-binding protein ParB, which condenses the centromeric regions of sister DNA molecules into kinetochore-like structures that recruit the DNA partition ATPase ParA and the prokaroytic SMC/condensin complex. Here, we report the crystal structure of a ParB-like protein (PadC) that emerges to tightly bind the ribonucleotide CTP. The CTP-binding pocket of PadC is conserved in ParB and composed of signature motifs known to be essential for ParB function. We find that ParB indeed interacts with CTP and requires nucleotide binding for DNA condensation in vivo. We further show that CTP-binding modulates the affinity of ParB for centromeric parS sites, whereas parS recognition stimulates its CTPase activity. ParB proteins thus emerge as a new class of CTP-dependent molecular switches that act in concert with ATPases and GTPases to control fundamental cellular functions.

Subfields: Genetics, Molecular Biology

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In Genetics

1. Lars-Oliver Essen
2. E. Krol
3. Anke Becker

In Molecular Biology

1. E. Krol
2. Anke Becker

Citations in the corpus

• Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, methodology): “0 software suites (both from Waters) as described previously (90).”