C-Terminal Globular Domain Of Gene Case Study

My gene is located at chromosome 9 on the long (q) arm at position 34, 9q34.

D1S80 locus is placed on the short arm of the chromosome 1. This locus does not code for the arrangement for protein, yet it codes for a series of tandem repeats of 16 bp in human. Distinctive number of this allele has different number of repeats. These quantities of repeats are exceptional to every human. Primer

UV radiation, such as that from the sun can be very harmful. It has been shown to cause many different mutations within cells, leading to issues for the organism such as death or disease. One of the most prevalent sources of UV radiation for humans is the sun. It’s very important for us to know the extent of cellular damage that can be caused by this radiation, as to know how harmful the sun’s rays are to us as humans. One way that the damage caused by the suns radiation can be tested is through the model organism yeast. For this lab, we exposed two different strains of yeast to UV radiation to test its affects. One strain was able to self-repair, while one was genetically altered so that it could not. Observations were recorded at

Second, in order to further confirm the information about characteristics and function of the targeting protein that we have

Duchenne Muscular Dystrophy is a sex-linked disease, which is inherited in a recessive fashion (National Human Genome Research Institute, 2013). Over thirty similar genetic disorders exist (Duchenne Foundation Australia, 2015). All types of muscular dystrophy are considered to be a rare disorder (Duchenne Foundation Australia, 2015). Duchenne Muscular Dystrophy is most common in children and causes muscle weakness and wasting, which commonly begins in the lower limbs (Duchenne Foundation Australia, 2015; National Human Genome Research Institute, 2013). The disease itself is caused by changes to the DMD gene, which is responsible for providing instructions regarding the creation of the dystrophin protein in one’s muscles (Duchenne Foundation Australia, 2015). This protein is responsible for protecting muscles from damage, and without it the cells of a person’s muscles deteriorate and symptoms of Duchenne Muscular Dystrophy are exhibited (Duchenne Foundation Australia, 2015). The disease results from changes in the DMD gene, or other genetic changes in a child (Duchenne Foundation Australia, 2015).

Duchenne Muscular Dystrophy is a sex-linked disease, which is inherited in a recessive fashion (National Human Genome Research Institute, 2013). Over thirty similar genetic disorders exist (Duchenne Foundation Australia, 2015). All types of muscular dystrophy are considered to be a rare disorder (Duchenne Foundation Australia, 2015). Duchenne Muscular Dystrophy is most common in children and causes muscle weakness and wasting, which commonly begins in the lower limbs (Duchenne Foundation Australia, 2015; National Human Genome Research Institute, 2013). The disease itself is caused by changes to the DMD gene, which is responsible for providing instructions regarding the creation of the dystrophin protein in one’s muscles (Duchenne Foundation Australia, 2015). This protein is responsible for protecting muscles from damage, and without it the cells of a person’s muscles deteriorate and symptoms of Duchenne Muscular Dystrophy are exhibited (Duchenne Foundation Australia, 2015). The disease results from changes in the DMD gene, or other genetic changes in a child (Duchenne Foundation Australia, 2015).

Each strain of muscular dystrophy is created by a genetic mutation distinct to that type. Duchenne’s has an absence of dystrophin, a protein that aids in keeping muscle cells together. Most of the mutations in the genes are inherited; some happen randomly in the mother’s egg (oocyte) or the developing embryo. Also, the mutations are able to be passed to the next generations.

Med. Genet 2009. 46, 825–833; Cardoso, C., Leventer, R.J., Ward, H.L., Toyo-Oka, K., Chung, J., Gross, A., Martin, C.L., Allanson, J., Pilz, D.T., Olney, A.H., et al. (2003). Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3. Am. J. Hum. Genet. 72, 918–930). MDS is caused by a heterozygous deletion of chromosome 17p13.3, involving several genes including PAFH1B1 and YWHAE coding for LIS1 and 14-3-3 proteins, respectively. This deletion induces malformations during cortical development (Dobyns, W.B., Stratton, R.F., Parke, J.T., Greenberg, F., Nussbaum, R.L., and Ledbetter, D.H. (1983). Miller-Dieker syndrome: Lissencephaly and monosomy 17p. J. Pedod. 102, 552–558; Chong, S.S., Pack, S.D., Roschke, A.V., Tanigami, A., Carrozzo, R., Smith, A.C.M., Dobyns, W.B., and Ledbetter, D.H. (1997). A revision of the lissencephaly and Miller-Dieker syndrome critical regions in chromosome 17p13.3. Hum.

An example of one such category of muscular dystrophy is distal muscular dystrophy. distal muscular dystrophy causes atrophied muscles due to a damaged DYSF or ANO5 gene. The DYSF gene aids in the creation of dysferlin. Dysferlin is found in the thin sarcolemma of the muscle tissue which is thought to aid the sarcolemma in repairing muscles. Since the production of dysferlin is inhibited by this form of muscular dystrophy, the muscles are not able to be repaired, leading them to become progressively more damaged and ineffective over time. Abnormalities in the other ANO5 gene, which produces anoctamin-5 affect muscles by reducing if not eliminating said protein. ANO5 is thought to provide transport for chlorine ions to the muscle cells of a muscle. These two genetic disorders are usually closely linked and it is common for the abnormality of one gene

What does the protein encoded by your gene do? What does it interact with? What biochemical pathway is it in? What biological function does

They are involved because the LMNA gene produces several slightly different proteins called laminas, of the major ones being Lamin A (also known as progerin) and Lamin C. These proteins are generally made throughout the whole body’s cells. The disease is causes the LMNA gene which to become mutated. Althought, this does not causes any harm to lamin c protein, it causes the lamin A protein to misshape, by missing out on 50 amino acids near one end. This is bad because the lamin A protein is a component the nuclear cell membrane. This misshaped version of lamin A is which is responsible for the disorder; it makes it so that it cannot be processed properly in a cell, which then causes a disrupted shape in the nuclear envelope. All in this mutation damages a cell’s structure and function to a nucleus which in turn causes the cells to die

mutation is phenylalanine 508 known as delta F508. Delta F508 is a deletion of 3 nucleotides

Nuclear Lamina is a mesh like network that lines the nuclear membrane and provides architectural support 2. Lamin proteins are important for cellular structure as well as cellular organization and because of this, functioning lamin proteins are vital in proper expression of genes 1. When mutated, lamin proteins lead to multiple degenerative diseases related to premature aging and diseases like progeria and muscular dystrophy. Although comprehensive research has been done on mutant lamin proteins, the relationship between genotypes and phenotypes are poorly understood 2. This proposal aims to analyze the different genotypic and phenotypic effects by

The Yeast two-hybrid system was used in this investigation to find which of four DNA inserts codes for a protein able to interact through protein-protein interactions with the protein encoded by the Bub1B gene. The protein encoded by the Bub1B gene is a kinase, which has a role in the formation of the mitotic spindle checkpoint ‘Davenporta et al. (1998)’

The Gene: Lamin A (LMNA), makes a protein that is required for holding the centre of the nucleus together. When it has been mutated (defect), an abnormal amount of the Lamin A protein called Progerin is produced and makes the cell unstable, this is what influences the diseases aging process.