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Lecture notes from week 7 of BISC 300

by: Jj Lynch

Lecture notes from week 7 of BISC 300 BISC300

Marketplace > University of Delaware > Biological Sciences > BISC300 > Lecture notes from week 7 of BISC 300
Jj Lynch

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About this Document

We didn't have class on Friday so here is Monday and Wednesday
Carlton Cooper
Class Notes
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This 3 page Class Notes was uploaded by Jj Lynch on Monday March 28, 2016. The Class Notes belongs to BISC300 at University of Delaware taught by Carlton Cooper in Summer 2015. Since its upload, it has received 13 views. For similar materials see Microbiology in Biological Sciences at University of Delaware.


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Date Created: 03/28/16
Monday Lecture Notes  Structure of DNA o Nucleotide polymer  Adenine, guanine, cytosine, thymine  Deoxyribose  Phosphate o Sugar and phosphate backbone, covalently bound 3’ C on sugar and 5’ C on sugar bond to phosphate  Replication in bacteria and eukaryotes pretty much the same o Helicase unwinds 2 strands and replication bubble travels down strands with polymerase Bacteria Eukaryotes Circular single DNA Linear DNA 1 replication fork Multiple fork 5 DNA polymerases (III is main) 3 DNA polymerase Telomeres at end of chromosome  Bacteria o DNA uses bidirection replication starting at origin of replication o Unwound at fork o Forks in eukaryotes and bacteria look similar o Primase lays down RNA primers, DNA polymerase (III) replaces RNA with DNA o DNA polymerase (I) replaces RNA primers with DNA o Polymerase works 5’-3’, adds to 3’ end o Leading strand = 3’-5’, lagging strand = 5’-3’ (has more primers) o Short segments of DNA on lagging strand = okazaki fragments  Ligase connects these strands together  DNA is transcribed into RNA (mRNA-messenger)  RNA uses ribose as sugar  Transcription o RNA polymerase unwinds DNA o Transcription bubble tracks with it and makes mRNA from template strand  Bubble holds temporary DNA;RNA hybrid Bacteria Eukaryotes 1 RNA polymerase 3 RNA polymerase Sigma factors Transcription factors Pribnow box TATA box Nucleoid region Nucleus Polycistronic mRNA Monocistronic mRNA (codes 1 protein) mRNA is processed (5’ cap, removal of introns, poly A tail)  Translation o mRNAamino acid sequence o codon=amino acid o codon is 3 base pairs o anticodon on tRNA (transfer) is complimentary to codon o start codon is start site, AUG o stop (nonsense) codon cause translation to stop and chain to be released o Ribosomes (70s) are protein and rRNA  Small subunit =30S, large =50S o Transfer RNA  Gets tertiary structure through base pairing  Has anticodon, binds to codon  3’ binds amino acid Bacteria Eukaryotes 30S+50S=70S ribosome 40S+60S=80S ribosome N-formylmethionine-tRNA Methionine-tRNA 3 release factors 1 release factor 3 initiation factors Much more Transcription and translation Separate simultaneous Nucleoid cytoplasm  small subunit binds mRNA, first tRNA binds, large subunit binds o hydrolysis of ATP happening to fuel  3 sites in large: EPA o first tRNA goes to P, ribosome moves, next tRNA binds to A, amino acid moves from P to A, ribosome shifts, empty tRNA goes to E, full tRNA is in P, continues until empty A site gets stop codon  3D shape determines protein function  after translation peptide chain is folded and associated with one or more proteins the delivered to place it is needed  molecular chaperones aid folding, protect cells from thermal damage ( ie/ heat shock proteins), and help move proteins across membranes Wednesday Lecture Notes  central dogma: DNARNAProtein  variations in genetic material give genetic diversity that is lacking in binary fission o mutations  vertical-can be spontaneous (error in replication) or induced (ie/ UV radiation)  horizontal-gene transfer (transformation, transduction, conjugation)  Mutation types o Point- can be transversion (purine to pyrimidine or vice versa) or transition (ie/ purine to purine)  Forward-progression towards change (evolution)  Silentno change in amino acid, just nucleotide  Missensechange in amino acid  Nonsensestop codon placed  Frameshiftreading frame shifted (from deletion or insertion)  Reverse-goes back to wild type from forward base substitution  Pseudo wild type if amino acid goes back to one with same properties (ie/ polar) but not the same amino acid  Suppressor-mutation suppresses another  ie/ deletion after insertion  Prototroph-is the wild type  Auxotroph-mutant  Replica plating can be used to detect auxotrophs o Find what amino acids the auxotroph needs to survive o Make media that only auxotroph will grow in  Carcinogenicity testing involves doing 1 culture with media, auxotroph and amino acid, on with mutagen added as well o See if more revertants induced by mutagen than compared to spontaneous (no mutagen)


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