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2018 ; 10
(4
): ä Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
Exploiting a Phage-Bacterium Interaction System as a Molecular Switch to Decipher
Macromolecular Interactions in the Living Cell
#MMPMID29614781
Surányi ÉV
; Hírmondó R
; Nyíri K
; Tarjányi S
; K?hegyi B
; Tóth J
; Vértessy BG
Viruses
2018[Apr]; 10
(4
): ä PMID29614781
show ga
Pathogenicity islands of Staphylococcus aureus are under the strong control of
helper phages, where regulation is communicated at the gene expression level via
a family of specific repressor proteins. The repressor proteins are crucial to
phage-host interactions and, based on their protein characteristics, may also be
exploited as versatile molecular tools. The Stl repressor from this protein
family has been recently investigated and although the binding site of Stl on DNA
was recently discovered, there is a lack of knowledge on the specific protein
segments involved in this interaction. Here, we develop a generally applicable
system to reveal the mechanism of the interaction between Stl and its cognate DNA
within the cellular environment. Our unbiased approach combines random
mutagenesis with high-throughput analysis based on the lac operon to create a
well-characterized gene expression system. Our results clearly indicate that, in
addition to a previously implicated helix-turn-helix segment, other protein
moieties also play decisive roles in the DNA binding capability of Stl.
Structural model-based investigations provided a detailed understanding of
Stl:DNA complex formation. The robustness and reliability of our novel test
system were confirmed by several mutated Stl constructs, as well as by
demonstrating the interaction between Stl and dUTPase from the Staphylococcal ?11
phage. Our system may be applied to high-throughput studies of protein:DNA and
protein:protein interactions.
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