Tryptophan is an essential amino acid, which is either synthesized or injested from the environment in bacterial cells.The production of tryptophan is an energy consuming process. So bacteria need to ensure that only when the concentration of tryptophan is low inside cell , it has to produce tryptophan. The trp operon is a repressible system that regulates the biosynthesis of tryptophan. The gene for the repressor is located not near to the promoter,but in a different location.It has an operator which is embedded in the promoter,a leader sequence(trpL) and 5 structural genes(trpE,trpD,trpC,trpB,trpA). Each gene encodes for proteins in the trp synthesis pathway. When the concentration of tryptophan is low there is no blockage for the transcription and tryptophan is produced. …show more content…
The mechanism of attenuation in trp operon
The process of controlling transcription termination by the rate of translation of the attenuator is termed as attenuation. In bacterial cells transcription and translation are coupled. The leader sequence (trpL) controls the operon through attenuation. The leader sequence has 4 main regions with some kind of palindromic sequence. When the amount of tryptophan is low the translation of domain1 (requires trp) slows down.The domains 2& 3 pairs which allows the continued transcription, resulting in the biosynthesis of tryptophan. At high concentrations of tryptphan , ribosome quickly moves through domain1 and associates with 2.This enables the strong pairing between domains 3&4.This pairing creates a stem and loop structure in the mRNA . This terminates transcription and the structural genes required for the tryptophan synthesis are not
Nucleolus- the nucleolus synthesizes ribosomal RNA (rRNA). Afterwards, these are put together with the proteins produced in the cytoplasm to create ribosomal units. 3. Nuclear Envelope-
After multiple cycles of ligation, detection and tail cleavages, the extended chain reached the end of the template. Then the whole extension chain is removed and a new starting primer switching down 1 nucleotide position binds onto the template for another cycle of reaction. Totally, five round of primer binding cycles are performed to complete the sequencing of each fragment. 3. Pitfalls and limitations of NGS Errors could be introduced in any step of the sequencing process, including library
A plasmid is a circular piece of DNA that contains genes that are not part of the original DNA of the bacteria. However, when a plasmid is inserted into a bacterial cell, its genes are transcribed and translated into proteins that the bacterial cell creates. In our experiment, we used the pGLO plasmid which encodes for a green fluorescent protein. These traits are visualized under a UV light; therefore, transformed bacterial cells will glow green when exposed to a UV light. 3.
The sucrose fermentation was a negative for acid meaning it was a red and a negative for gas. The H2S production was a negative because remained a yellow color instead of turning black. For the motility, it was also a negative the movement only stayed in the center than spreading throughout. The indole from tryptophan was also a negative because no ring appeared on the top layer on the reagent.
Genetic transformation is portrayed simply as a ”’change caused by genes’” (DNA) from an external source, which alters the traits within an organism ("pGLO Transformation,"). In this lab, a bacterium called Escherichia coli (E. coli) will be transformed utilizing a gene that codes for Green Fluorescent Protein (GFP) (Urnowey et al., 2017). This particular gene (GFP) comes from the bioluminescent jellyfish, Aequorea victoria, where the protein enables the jellyfish to glow in the dark ( Urnowey et al., 2017). Likewise, if the transformation experiment is done effectively, the bacterial cell, E. coli, will inherit the GFP gene and exhibit the same glow found in the jellyfish (Urnowey et al., 2017).
Genetic disorders booklet: polydactyly Q. Who first discovered the genetic disorder? How was it discovered? A. Tyler Steven Hayden was the one who discovered the disorder.
According to the article called “ Free L-Trytophan plasma levels in antisocial violent offenders” by Jari Tilhonen, Multi Virkkunan, Pirkka Rusanen, Sirrjoa Pennanen, Eevarliisa Sainio, james Callaway, Pirjo Halonwn, and Jyrki Liesiviuori, they stated that tryptophan is the dietary precursor of serotonin and a deficiency is either tryptophan intake or it is metabolism which can cause mental disorders. (Tihonen, Virkkunan, Rusanen, Pennnanen, Sainio, Callaway, Halonwn, &Liesiviouri, 2013). In the past, it was several studies that reported that depressed individuals have low tryptophan. Lucca et al had discovered in their case study that violent offenders have low levels of L-tryptophan and plasma levels.
The ability to recognize specific proteins in the cell has advantages on understanding how the cell functions. Its importance of protein-identifying techniques can detect the presence of many genetic disorders. The purpose of this experiment is to determine the effects of heat shock stress proteins in E. coli. To approach this lab, heat shock the proteins and measure total protein levels. Use two different techniques to run the gels.
The transposon of Tn4351 was originally detected in E. coli which carried an unstable chimeric plasmid, pSS-2. The mobilization of pSS-2 from onestrain of E. coli
3. How is DNA information used to synthesize polypeptides? A gene or protein is used to make polypeptides. In order to create this gene, transcription and translation must take place to create a protein from DNA.
However, all proteins are constructed from the same set of 20 amino acids linked in unbranched polymers. The covalent bond that exists between amino acids is called peptide bond, hence a polymer of amino acids is named polypeptide. A protein is a biological functional molecule made up of one or more polypeptides which is folded and coiled into unique three-dimensional structure. In laboratory, it is important to measure the concentration of proteins for research investigations. Biuret test is adopted to quantify proteins in fluid by using a spectrophotometer.
A group of 3 nucleotides is called codons. Each codon on the mRNA molecule matches a corresponding anti-codon on the base of a tRNA molecule. The tRNA anti-codon attaches to the mRNA codon. Then, the larger subunit of the ribosome disconnects an amino acid from a corresponding tRNA molecule and adds it to the growing protein chain. When the mRNA is completely decoded a protein is made
Additionally, there exists three domains of the enzyme namely C- terminal catalytic domain, an N- terminal regulatory domain and a tetramerization domain. Tetrahydrobiopterin (BH4) acts as a cofactor for the enzyme activity. Hence, the regulatory action by PAH enzyme involves activation by the presence of the amino acid phenylalanine, inhibition by the cofactor Tetrahydrobiopterin (BH4) and activation of the enzyme by phosphorylation. Cyclic adenosine monophosphate (cAMP) – dependent protein kinase helps in the phosphorylation of the amino acid serine that is present on the 16 position of the regulatory domain of the enzyme. This in turn helps in maintaining the activity of the enzyme by reducing the concentration of the phenylalanine
The enzymes responsible are Glycogen synthase and branching enzyme.
These enzymes are similar to traffic lights. They can slow, speed up and stop metabolic processes. If a cells metabolic pathways were not regulated well, the chemical chaos would occur. Most of metabolic processes take place non-spontaneously, enzymes help make those chemical