1. Given the MRNA: 5'AUGCAUGACGAUCUCGUCGCG...3' a. Use the genetic code to predict the amino acid sequence encoded by the mRNA. b. Naturally, the information in this MRNA came from DNA. Give the sequence of the sense strand of the DNA.
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- 2) Myoclonal epilepsy and ragged red fiber disease (MERRF) is a human condition named for the ragged red fibers of skeletal muscle cells and myoclinic epilepsy in affected individuals. People with this disorder have a mutation in a mitochondrial gene for a tRNA, specfically that for lysine. Why are affected individuals always heteroplasmic?2a) In prokaryotes, a small ribosomal subunit can potentially get on an mRNA anywhere it can find enough space to do so. Once a small ribosomal subunit has bound to an mRNA, it will scan along that mRNA in the 5' to 3' direction looking for a start codon at which to initiate translation. How does the small ribosomal subunit distinguish a start codon from any other AUG codon that simply codes for methionine in the middle of a coding sequence?A normal mRNA that reads 5’ - UGCCAUGGUAAUAACACAUGAGGCCUGAAC- 3’ has an insertion mutation that changes the sequence to 5' -UGCCAUGGUUAAUAACACAUGAGGCCUGAAC- 3’. Translate the original mRNA and the mutated mRNA, and explain how insertion mutations can have dramatic effects on proteins. (Hint: Be sure to find the initiation site.)
- A fragment of bacterial DNA reads: 3’ -TACCTATAATCTCAATTGATAGAAGCACTCTAC- 5’ Assuming that this fragment is the template strand, what is the sequence of mRNA that would he transcribed? (Hint: Be sure to identify the initiation site.)Amino acids are not stored in the body. Describe how excess amino acids are processed in the cell.The Second Genetic Code Review the evidence establishing that aminoacyl-tRNA synthetases bridge the information gap between amino acids and codons. Indicate the various levels of specificity possessed by aminoacyl-tRNA synthetases that are essential for high-fidelity translation of messenger RNA molecules.
- 14. Which mutation would be more harmful to a cell? For each predict the outcome of each mutation and explain one is worse than the other A) A mutation in the anticodon of Ala-tRNA from IGC to IGG OR a mutation in the alanyl tRNA synthase such that it adds either Ala or Ile to the appropriate tRNA? B) A mutation in bases 11 and 24 of the Ser-tRNA (both important recognition elements for serinyl tRNA synthase OR a mutation in the proofreading site of serinyl tRNA that inactivates proofreading2) Myoclonal epilepsy and ragged red fiber disease (MERRF) is a human condition named for the ragged red fibers of skeletal muscle cells and myoclinic epilepsy in affected individuals. People with this disorder have a mutation in a mitochondrial gene for a tRNA, specifically that for lysine. Why are affected individuals are always heteroplasmic?38. Assume that the reading frame is from left to right and that the columns represent transcriptional and translational alignments. Use the provided Genetic Code table.
- Choose the correct option for following three mcqs 7.The first step in the capping reaction is catalyzed by: Phosphatase Guanylyl transferase Methyl transferase Kinase None of the above 8.Which of the following statements about tRNAs is FALSE? They contain an anti-codon loop They contain several modified bases Their secondary structure looks like a cloverleaf They are generally less then 100 nucleotides in length They are synthesized by RNA polymerase-II 9.During protein synthesis _____ delivers the charged tRNA to the A-site. EF-Tu EF-G eIF-2 RF1 RF222-69 Indicate whether each of the following statementsrelating to protein synthesis is true or false.a. RNA is involved in both the transcription andtranslation phases of protein synthesis.b. DNA is the starting material for protein synthesis.c. The translation phase of protein synthesis convertsRNA to DNA.d. Transcription precedes translation in proteinsynthesis15. Cellular proteins are oftentimes post-translationally modified. Choose one of the following PTMs: N-linked glycosylation, phosphorylation, ubiquitination, or GPI-anchor. Clearly indicate your choice, then address the following: (a) How is the PTM attached to the protein of interest? At which amino acid residue(s)? What enzyme(s) is involved, if any? (b) Is the PTM relatively stable or highly dynamic? Explain. How does the PTM become detached from the protein of interest? What enzyme(s) is involved, if any? (c) What is the function of the PTM? Provide one specific example.