Deciphering such interactions is of paramount importance for a better understanding of virus infection cycles and the development of new strategies for virus prevention and control. ![]() Productive viral infection entails highly regulated and sequential protein–protein interactions between viral factors and between virus and host factors. (Reprinted from with permission from the American Chemical Society) SH2 Src SH2 domain of Src protein, ER LBD ER ligand binding domain, CB Red-N N-terminal domain of red click beetle luciferase, CB Red-C C-terminal domain of red click beetle luciferase, CB Green-N N-terminal domain of green click beetle luciferase, LXXLL motif amino acid sequence interacting with The ER ligand binding domain for genomic activities of ligands. Depending on the type of agonist or antagonist and initiation of either genomic or nongenomic pathway, red or green bioluminescent signals will be detected as a result of complementation of the C-terminal fragment and each of the two N- terminal fragments. Two N-terminal fragments of luciferase emitting different colors (red and green) and one C-terminal fragment are alternatively embedded among the fragments mentioned. Here, a multicolor probe is designed by fusing the ligand binding domain of an estrogen receptor (ER) and the two probable different interacting motifs of the SH2 domain and LXXLL. Ntegrated-molecule-format multicolor probe for detecting multiple activity of an active small molecule. ![]() We review the various applications of this novel luminescent biosensor in studying protein-protein interactions and assaying metabolites involved in analytical biochemistry, cell communication and cell signaling, molecular biology, and the fate of the whole cell, and show that luciferase-based biosensors are powerful tools that can be applied for diagnostic and therapeutic purposes. Split luciferase is an effective tool for assaying biochemical metabolites, where a domain or an intact protein is inserted into an internally fragmented luciferase, resulting in ligand binding, which causes a change in the emitted signals. On interaction of those proteins, luciferase fragments are placed close to each other and form a complemented luciferase, which produces a luminescent signal. In this technique, each of the two domains of luciferase is attached to each partner of two interacting proteins. The split-luciferase complementation assay makes the study of two or more interacting proteins possible. These protein-protein interactions are vital to facilitate the biological activity of cells. These molecular complexes are built from a few to many proteins organized through their interactions. ![]() Biochemical events are mostly accomplished through large protein machines. Bioluminescent systems are considered as potent reporter systems for bioanalysis since they have specific characteristics, such as relatively high quantum yields and photon emission over a wide range of colors from green to red.
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