Proteins are the most critical executive molecules by responding to the instructions stored in the genetic materials in any form of life. More frequently, proteins do their jobs by acting as a roleplayer that interacts with other protein(s), which is more evident when the function of a protein is examined in the real context of a cell. Identifying the interactions between (or amongst) proteins is very crucial for the biochemistry investigation of an individual protein and for the attempts aiming to draw a holo-picture for the interacting members at the scale of proteomics ( or protein-protein interactions mapping). Here, we introduced the currently available reporting systems that can be used to probe the interaction between candidate protein pairs based on the fragment complementation of some particular proteins. Emphases were put on the principles and details of experimental design. These systems are dihydrofolate reductase (DHFR), β-lactamase, tobacco etch virus (TEV) protease, luciferase, β-galactosidase, GAL4, horseradish peroxidase (HRP), focal adhesion kinase (FAK), green fluorescent protein (GFP), and ubiquitin.
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Ribosome is primarily regarded as the committing organelle for the translation process. Besides the expansion of
its function from a translational machine for protein synthesis to a regulatory platform for protein quality control, the
activity regulation and recycling of ribosome have been deepened significantly. Recent advances have confirmed a novel
mechanism in the regulation of ribosome activity when a cell encounters adverse conditions. Due to the binding of certain
protein factors onto a ribosome, the structural and functional change of the ribosome inside the cell will take place, thereby
leading to the formation of inactive ribosomes (70S monomer or 100S dimer), or ribosome hibernation. By ribosome
hibernation, the overall protein synthesis rate of a cell could be slowed down. The resistance to adverse conditions or
chemicals of the host cell will be enhanced. In this paper, we discussed the phenomenon, molecular mechanism, and
physiological effect of ribosome hibernation when cells are under stresses. And then, we discussed the resuscitation of a
hibernating ribosome and the role of ribosome hibernation in the treatment of antimicrobial infection.
Transcription can be regulated by controlling the provision of transcriptional factors (TFs), because TFs determine the transcription process by specifying the binding of RNA polymerase holoenzyme on promoters. Manipulations, such as replacing endogenous TFs with mutants obtained through directed evolution (or rational design), and introducing compatible heterogeneous TFs, are effective ways to regulate transcription. Designing artificial TFs with desired properties by following the principles of protein design and reconstructing ancestral TFs with the information gained from a perspective of evolution by multiple sequence alignments of the related TFs, are feasible alternative options. The engineered TFs can be used to create inducible protein expression systems that respond to a specific stimulus. Moreover, the engineered TFs could lead to a transcriptional profile different from that of the wild-type strains. Accordingly, these engineered TFs could be utilized to construct strains resistant to adverse conditions, since the emergence of resistance generally requires global transcriptional changes at the transcriptomic scale. Meanwhile, these engineered TFs can also be employed in the construction of sophisticatedly designed genetic circuits for diverse purposes. In this paper, we reviewed the advances in the above-mentioned aspects.
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