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Chemically induced dimerization (CID) is a biological mechanism in which two proteins bind only in the presence of a certain small molecule, enzyme or other dimerizing agent. [1] Genetically engineered CID systems are used in biological research to control protein localization, to manipulate signalling pathways and to induce protein activation.
Traditionally the measure of gene products (i.e. mRNA, proteins, etc.) has been the major approach of measure promoter activity. However, this method confront with two issues: the stochastic nature of the gene expression [5] and the lack of mechanistic interpretation of the thermodynamical process involved in the promoter activation. [4]
Gal4 is a modular protein consisting broadly of a DNA-binding domain and an activation domain. The UAS to which GAL4 binds is CGG-N 11-CCG, where N can be any base. [6] Although GAL4 is a yeast protein not normally present in other organisms it has been shown to work as a transcription activator in a variety of organisms such as Drosophila, [7] and human cells, highlighting that the same ...
Tetracycline-controlled transcriptional activation is a method of inducible gene expression where transcription is reversibly turned on or off in the presence of the antibiotic tetracycline or one of its derivatives (e.g. doxycycline).
Activation-induced cytidine deaminase, also known as AICDA, AID and single-stranded DNA cytosine deaminase, is a 24 kDa enzyme which in humans is encoded by the AICDA gene. [5] It creates mutations in DNA [ 6 ] [ 7 ] by deamination of cytosine base, which turns it into uracil (which is recognized as a thymine ).
The GUS system is not the only available gene reporter system for the analysis of promoter activity. Other competing systems are based on e.g. luciferase, GFP, beta-galactosidase, chloramphenicol acetyltransferase (CAT), alkaline phosphatase. The use of one or the other system is mainly dependent on the organism of interest and the imaging and ...
Two-hybrid screening (originally known as yeast two-hybrid system or Y2H) is a molecular biology technique used to discover protein–protein interactions (PPIs) [1] and protein–DNA interactions [2] [3] by testing for physical interactions (such as binding) between two proteins or a single protein and a DNA molecule, respectively.
After activation, is a tetramer with a molecular weight around 100 kD. [20] However, the form of enzyme present in the circulation does not correspond to the protein as encoded by the gene: the main fraction of the active enzyme in the circulation has a molecular weight of 730 kD and is probably bound in a complex to other proteins.