What is GFP in Drosophila?
Abstract. We have used the green fluorescent protein (GFP) from the jellyfish Aequorea victoria as a vital marker/reporter in Drosophila melanogaster. Transgenic flies were generated in which GFP was expressed under the transcriptional control of the yeast upstream activating sequence that is recognized by GAL4.
What is the function of the GFP marker gene?
Biologists use GFP as a marker protein. GFP can attach to and mark another protein with fluorescence, enabling scientists to see the presence of the particular protein in an organic structure. Gfp refers to the gene that produces green fluorescent protein.
How do you tag a gene with GFP?
Popular Answers (1)
- Use a vector, place your gene in front of the GFP gene. The stop codon of your gene should be removed, and your gene and the GFP gene should be in frame.
- Attached a paper for you.
- Also refer to another RG post for the similar topic with other persons’ suggestions.
What activates the GFP gene?
In A. victoria, GFP fluorescence occurs when aequorin interacts with Ca2+ ions, inducing a blue glow.
What is a protein trap?
Protein-trap is a method that allows for the identification of proteins of interest based on their unique subcellular localization without the use of specific antibodies to each protein.
Why is GFP so widely used?
The gfp gene is widely used as a marker because of its very useful properties such as high stability, minimal toxicity, non-invasive detection and the ability to generate the green light without addition of external cofactors and without application of expensive equipment.
How do GFP plasmids work?
Green fluorescent protein (GFP) is a protein that causes the Aequorea victoria jellyfish to glow. The protein is coded for by a single gene. The GFP gene can be inserted downstream of the promoter of a gene in another organism. RNA polymerase binds to promoter regions to initiate transcription.
How does GFP fluorescence work?
GFP is a barrel shape with the fluorescent portion (the chromophore) made up of just three amino acids. When this chromophore absorbs blue light, it emits green fluorescence.
Why is GFP fluorescent?
What is the source of the GFP fluorescence?
3.19. Green fluorescent protein (GFP) was originally derived from the jellyfish Aequorea victoria (Prendergast and Mann, 1978). It has 238 amino acid residues and a green fluorophore, which is comprised of only three amino acids: Ser65-Tyr66-Gly67.
Is there an alternative to actin-GFP for visualising actin structure and dynamics?
Recently LifeAct-GFP (green fluorescent protein) has been proposed for visualising actin structure and dynamics in live cells as an alternative to actin-GFP which has been shown to affect cell mechanics. Here we compare the two approaches in terms of their effect on cellular mechanical behaviour.
What happens when drosophilamyosin VI is reduced?
In Drosophilamyosin VI mutants in which the expression of myosin VI is greatly reduced in the testis, actin cone organization is disrupted and individualization stops prematurely (Hicks et al., 1999). In wild-type testes, myosin VI localizes at the fronts of actin cones.
What happens to actin density during Myosin VI overexpression?
In the mutant, both total amount and the density of actin declined to about half of their premovement level once movement began (Figure 3, C and D). In the myosin VI overexpression line (Figure 3E), actin cones were similarly shaped as wild-type, and they initially had similar actin content.
What is the function of the actin cytoskeleton?
The actin cytoskeleton forms a dynamic structure involved in many fundamental cellular processes including the control of cell morphology, migration and biomechanics.