New paper published in Structural Chemistry

Written on 21 September 2015.

Our paper entitled "Exploring the role of the phage-specific insert of
bacteriophage Φ11 dUTPase" has been published in Structural Chemistry.



dUTPases are essential for maintaining genome integrity. Recently, in the
case of a dUTPase from a Staphylococcal phage, another different
physiological function was also suggested. Namely, it was shown that
dUTPase from the Staphylococcus aureus bacteriophage Ф11 is capable of
binding to the Staphylococcal Stl repressor protein. This binding
interferes with the function of Stl. In the present study, we investigated
the putative role of a phage dUTPase-specific peptide segment in the
interaction of dUTPase with Stl and in impeding Stl–DNA complex formation.
We show that dUTPase from Mycobacterium tuberculosis that lacks the
phage-specific insert is also capable of disrupting the complexation
between Stl and DNA. Hence, the insert segment is not essential for
perturbation of the Stl function. However, we also demonstrate that in case
of the phage dUTPase, the insert-lacking construct is deficient in
perturbation of Stl activity. These findings clearly indicate that the
phage-specific insert has a well-defined role only in the context of the
phage dUTPase.

Structural Chemistry, 30 August 2015, doi: 10.1007/s11224-015-0652-2

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