Microbiology news and views
J. Mol. Micro. Biotechnol. 3: 73-82
Protein-Protein Interaction Between Bacillus
stearothermophilus Tyrosyl-tRNA Synthetase Subdomains Revealed by a Bacterial Two-Hybrid System
Gouzel Karimova, Agnes Ullmann and Daniel Ladant
We have recently developed a bacterial two-hybrid system (BACTH), based on functional complementation between two fragments of the catalytic domain of
Bordetella pertussis adenylate cyclase (AC), that allows an easy
in vivo screening and selection of functional interactions between two proteins in
Escherichia coli. In this work, we have further explored the potentialities of the BACTH system to study protein-protein interactions, using as a model, the interactions between various
subdomains of the dimeric tyrosyl-tRNA synthetase (TyrRS) of
Bacillus stearothermophilus. Using the BACTH system we confirmed the known interactions of the
a/b domains and those between the a/b domain and the
a domain that could be anticipated from the three-dimensional structure of TyrRS. Interestingly, the BACTH system revealed
the unexpected interaction between the TyrRS a domains which is presumably mediated by a pseudo-leucine zipper motif. This study illustrates the interest of
the bacterial two-hybrid system to delineate interacting domains of proteins and shows that it can reveal interactions that occur
in vivo and that were not anticipated from the three-dimensional structure of the protein of interest.
Full article [pdf]
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