GEN 3000: EXAM 4 Study Guide
GEN 3000: EXAM 4 Study Guide GEN 3000
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This 4 page Study Guide was uploaded by Jomary Arias on Saturday April 2, 2016. The Study Guide belongs to GEN 3000 at Clemson University taught by Dr. Kate Tsai in Spring 2016. Since its upload, it has received 139 views. For similar materials see Genetics in Biomedical Sciences at Clemson University.
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Date Created: 04/02/16
GEN 3000: EXAM 4 STUDY GUIDE CHAPTERS 13-15 CHAPTER 13 Chapters Terms Topics [Key Terms] Ribosomes- the protein synthesis machines are made up of protein and RNA. tRNA Charging- RNA that has an amino acid attached to it and binds to the codon on the mRNA. Aminoacyl- tRNA synthetase- key enzyme that brings together the correct amino acids and correct tRNA. Initiation- components such as mRNA, small and large ribosomal subunits, and initiator tRNA begin to assemble IF-3- binds to small subunit, blocks large subunits from binding to small subunit. Allows small subunit to attach to mRNA Shine Delgarno- in bacteria transcripts the small subunit binds Translation- performed by the ribosome by reading mRNA and synthesizing the protein Termination- translation happens when ribosome hits a STOP codon on the mRNA IF-1- enhances dissociation of large and small ribosomal subunits Kozak- sequence can surround start in eukaryotes, only for select genes Poly A tail- at 3’ end of mRNA also plays a role by enhancing binding of the small subunit of ribosome to mRNA. Antibiotics- can target differences b/w prokaryotic and eukaryotic mechanisms [Ribosomes] - One of the most abundant organelles in the cell - Contains 80% pf cellular RNA - Made up of 50 different proteins and RNA molecules - Consist of large & small subunits [Initiation] 3 Steps: 1. mRNA binds to SMALL ribosomal subunit 2. Initiator tRNA binds to mRNA 3. LARGE ribosome joins initiator complex [Elongation] 3 Steps: GEN 3000: EXAM 4 STUDY GUIDE CHAPTERS 13-15 1. Delivery of charged binding tRNA to A site, requires Ef-Tu, EF-T, and GTP. 2. Formation of a peptide bond b/w adjacent amino acids in P and A sites. Releases amino acids in P site. 3. Translation- Movement of the ribosome to the next codon, occurs one codon at a time until a STOP codon is reached. [Protein Structure] 4 Steps: 1) Primary- sequence of amino acids 2) Secondary- interaction b/w amino acids create folds and twists of polypeptide. There are two main shapes: (1) Beta sheets, (2) Alpha helix 3) Tertiary- interaction of secondary structures form a 3D shape 4) Quaternary- when two or more polypeptides interact CHAPTER 14 [Key Terms] Mutation- inherited change in genetic information (either in daughter cells or in individuals). Also causes genetic variation, usually BAD! Ames Test- used to identify potential mutagens Transposable Elements- jumping genes or mobile DNA that causes repetition, accounts for 50% of human genome Somatic Mutations- arise in somatic (non-sex) cells and are passed to daughter cells by mitosis. Germ-Line Mutations- arise in cells that make gametes and are passed to future generations Spontaneous Mutations- changes in nucleotide sequence that occur w/ no known cause. Ex) Replication errors Induced Mutations- changes that occur as the result of outside factors which can be natural or artificial. Ex) UV radiation Base/Base Pair Substitution- alteration of a single nucleotide, when one is altered the base of the corresponding nucleotide on other strand is also impacted (a) Transition- like replaces like, purines replace purines (b) Transversion- purines replace pyrimidine Insertion/ Deletion- most frequent form of mutations, can cause frameshift mutations in coding regions of proteins Forward Mutations- changes wild-type allele GEN 3000: EXAM 4 STUDY GUIDE CHAPTERS 13-15 Reverse Mutations- changes a mutant allele back to wild-type Loss-of-Function Mutations- alters protein so much that it doesn’t work and becomes a null protein Gain-of-Function Mutations- produces new traits Suppressor Mutations- hides the impact of another mutation Visible- easily observed. Ex) Pigmentation Nutritional- loss of ability synthesize an amino acid or vitamin Biochemical- mutation in a biochemical pathway Behavioral- changes behavior patterns Regulatory- changes gene expression, can disrupt an entire pathway Lethal- disrupts an essential process Conditional-only expressed under certain environmental conditions Temperature-Sensitive- variable function at different temperatures [Transposition characteristics] 1) Staggered breaks are made in DNA 2) TE is joined in the ssDNA ends of target 3) DNA is replicated at gapes to repair (creating flanking direct repeats Ac Element Ds Element -ACTIVATOR -DISSOCIATION, non-autonomous and -Autonomous and can transpose cannot transpose alone. -Are smaller because they have deletions which wipe out the function of transposase. LINEs SINEs Long interspersed nuclear elements- Short interspersed nuclear elements, encode own reverse transcriptase lack RT 1-5 kb in length 100- 300 bp 20,000-40,000 copies in human 1.5 million in human genome genome Most common transposable element in the human is Alu element GEN 3000: EXAM 4 STUDY GUIDE CHAPTERS 13-15 CHAPTER 15 [Key Terms] Constitutive Enzymes- always produced Adaptive/ Facultative Enzymes- made when needed Inducible- production is “on” when an inducer is present. Ex) lac operon Repressible- production is “off” when a product is present. Ex) trp operon Operon- single transcriptional unit, contains series of genes, a promoter, and an operator Transcriptional Control- can be negative or positive CAP- catabolite activator protein, enhances RNA pol binding to promoter Positive Regulation Negative Regulation -Uses an ACTIVATOR to help transcription - Uses a REPRESSOR to help prevent occur transcription from occurring -Activator can be either: Inducible -OR- -Repressor can be either: Inducible –OR- Repressible Repressible
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