Structural analysis and knock-out of a Burkholderia pseudomallei homolog of the eukaryotic transcription coactivator PC4

- Crystal structures of a putative PC4 homolog from Burkholderia pseudomallei were solved.
- Conserved structural features suggest a DNA-binding mode similar to that of PC4.
- Knock-out and complementation phenotypes argue against a role in repair and oxidative stress.
- Results may reflect redundancy or a bacteriophage origin of Burkholderia PC4 homologs.

Homologs of the eukaryotic transcription coactivator PC4, which also functions in DNA repair and oxidative stress, were recently identified in prokaryotes. Crystallographic analysis of BPSL1147, a putative homolog from the pathogen Burkholderia pseudomallei K96243, reveals a highly conserved core structure and suggests a nucleic acid binding mode similar to that of PC4. Knock-out and complementation experiments do not reveal distinguishing phenotypes under normal growth conditions or in the presence of H2O2, arguing against a critical role in repair or the oxidative stress response of Burkholderia. These results may reflect redundancy or point at a bacteriophage origin of Burkholderia PC4 homologs.

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