The human genome does not encode substantially more protein domains than do invertebrate genomes, yet it encodes many more proteins. How are more proteins encoded when the number of domains does not differ substantially?
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The human genome does not encode substantially more protein domains than do invertebrate genomes, yet it encodes many more proteins. How are more proteins encoded when the number of domains does not differ substantially?
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- What are paralogous and orthologous genes? What are some of the explanations for the finding that humans are a much more complex organism than the roundworm C. elegans, yet have only about 5 percent more protein- coding genes (21,000 versus 20,000)?Antibiotics such as chloramphenicol, tetracycline, and erythromycin inhibit protein synthesis in bacteria, but have no effect on the synthesis of proteins encoded by eukaryotic nuclear genes. Cycloheximide inhibits the synthesis of proteins encoded by nuclear genes, but has no effect on bacterial protein synthesis. How might these compounds be used to determine which proteins are encoded by mitochondrial and chloroplast genomes?Dystrophin is a protein that forms part of a vital protein complex that connects the cytoskeleton of a muscle fiber cell to the extracellular matrix. This connection strengthens and shapes the muscle fibers. Dystrophin is coded by the DMD gene. This is one of the longest human genes known, covering 2,300,000 base pairs (0.08% of the human genome) It is located in chromosome 21. The immature mRNA is 2,100,000 bases long and takes 16 hours to transcribe. It contains 79 exons. The mature mRNA measures 14,000 and codes for a protein with 3,685 amino acids. Abnormal expression of dystrophin leads to severe symptoms like muscle weakness and fatigability, a disease that is called muscular dystrophy. Most patients with muscular dystrophy become wheelchair dependent early in life. Cardiac muscle is also affected which results typically in premature death (~ second or third decade of life). Several mutations in this gene have led to the production of low levels of dystrophin or of a defective,…
- A hereditary disease is inherited as an autosomal recessive trait. The wild-type allele of the disease gene produces a mature mRNA that is 1250 nucleotides (nt) long. Molecular analysis shows that the mature mRNA consists of four exons that measure 400 nt (exon 1), 320 nt (exon 2), 230 nt (exon 3), and 300 nt (exon 4). A mother and father with two healthy children and two children with the disease have northern blot analysis performed. The results of the northern blot for each family member are shown below. a) Identify the genotype of each family member, using the size of mRNAs to indicate each allele. (For example, a person who is homozygous wild type is 1250/1250). b) Based on your analysis, what is the most likely molecular abnormality causing the disease allele?Consider Molecule X, which is found in all living cells. This molecule is transcribed from a stretch of DNA in the nucleus. Each nucleobase on the DNA produces a matching nucleobase on this molecule. Every 3-base codon specifies an amino acid in a protein. What is the name of X? Your answer should be one word, or a short two- or three-word phrase. Spelling counts. Note: if there is more than one possible answer, separate each answer with a comma. x 5What are some reasons why, in multicellular eukaryotes, genome size is not necessarily related to number of protein-coding genes or organismal complexity?
- Duchenne muscular dystrophy (DMD) is an X-linked recessive genetic disease caused by mutations in the gene that encodes dystrophin, a large protein that plays an important role in the development of normal muscle fibers. The Dystrophin gene is immense, spanning 2.5 million base pairs, and includes 79 exons and 78 introns. Many of the mutations that cause DMD produce premature stop codons, which bring protein synthesis to a halt, resulting in a greatly shortened and nonfunctional form of dystrophin. Some geneticists have proposed treating DMD patients by introducing small RNA molecules that cause the spliceosome to skip the exon containing the stop codon (A. Goyenvalle et al., 2004. Science 306:1796–1799). The introduction of the small RNAs will produce a protein that is somewhat shortened because an exon is skipped and some amino acids are missing, but it may still result in a protein that has some function. The small RNAs, antisense RNAs, used for exon skipping are complementary to…Another way to study the role of proteins (e.g., transcription factors) that function in development is to microinject the mRNA that encodes a protein, or the purified protein itself, into an oocyte or embryo, and then determine how this affects the subsequent development of the embryo, larva, and adult. For example, if Bicoid protein is injected into the posterior region of an oocyte, the resulting embryo will develop into a larva that has anterior structures at both ends. Based on your understanding of the function of each developmental gene, what would be the predicted phenotype if the following proteins or mRNAs were injected into normal oocytes? A. Nanos mRNA injected into the anterior end of an oocyte B. Antp protein injected into the posterior end of an embryo C. Toll mRNA injected into the dorsal side of an early embryoWhat percentage of the human genome is nowpredicted to have functionality in at least one cell type?
- Duchenne muscular dystrophy (DMD) is an X-linked recessive genetic disease caused by mutations in the gene that encodes dystrophin, a large protein that plays an important role in the development of normal muscle fibers. The dystrophin gene is immense, spanning 2.5 million base pairs, and includes 79 exons and 78 introns. Many of the mutations that cause DMD produce premature stop codons, which bring protein synthesis to a halt, resulting in a greatly shortened and nonfunctionalform of dystrophin. Some geneticists have proposed treating DMD patients by causing the spliceosome to skip the exon containing the stop codon. Exon skipping would produce a protein that is somewhat shortened (because an exon is skipped and some amino acids are missing), but might still result in a protein that had some function (A. Goyenvalle et al. 2004. Science 306:1796–1799). Propose a possible mechanism to bring about exon skipping for the treatment of DMD.One of the two genes known to be mutated in cases of Hypokalemic periodic paralysis (which is inherited in an autosomal dominant pattern but known to affect males more often than females) is the calcium voltage-gated channel subunit alpha1 S (CACNA1S). What is known about the gene is recorded here: https://www.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000081248;r=1:201039512-201112451 Please navigate to the link above and use the information and link-outs from the page to answer the following question. GIVE YOUR ANSWER AS A NUMBER ONLY, NO UNITS: What is the size in amino acid residues of the CACNA1S transcript named CACNA1S-202? Answer: The size of the CACNA1S transcript named CACNA1S-202 is how many amino acid residues.One of the two genes known to be mutated in cases of Hypokalemic periodic paralysis (which is inherited in an autosomal dominant pattern but known to affect males more often than females) is the calcium voltage-gated channel subunit alpha1 S (CACNA1S). What is known about the gene is recorded here: https://www.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000081248;r=1:201039512-201112451 Please navigate to the link above and ensure that you click to reveal the transcript table. Then use the information in the table to answer the following question. PLEASE GIVE YOUR ANSWER AS A NUMBER ONLY, NO UNITS What is the size in base pairs of the CACNA1S transcript named CACNA1S-202? Answer: The size of the CACNA1S transcript named CACNA1S-202 is