MedCom's Notes For STORAGE & EXPRESSION OF GENETIC INFORMATION RNA & Protein Synthesis TYPES Ribosomal RNA:

: With ribosomes,protein synthesis,80% of all Prokaryotic 23,16,5 Eukaryotic28,18,5.8, 5s With catalytic activity is ribozyme Transfer RNA: Smallest (4s) Each amino acid have its own tRNA,15% of all, Increase unusual base pairing secondary & tertiary structure Messenger RNA 5%,most heterogenous type Poly-cistronic Carry info from more than 1 gene Mono-cistronic Carry info from 1 gene Poly A tail on 3 end , 7 methyl-guanosine cap at 5 end TRANSCRIPTION OF PROKARYOTIC RNA A: prokaryotic RNA polymerase All RNA are synthesized by RNA polymerase except RNA primer RNA polymerase recognise promoter region 2 alpha,1 beta,1 beta template binding Alpha=enzyme assembly Beta=53 poly activity sigma factor holoenzyme helps RNA polymerase B: steps 1. Initiation: RNA poly binds with promoter(which is not transcribe) -35 TTGACA -10 TATAAT Pribnow box 2. Elongation: RNA poly dont have proofreading & dont require primer, after 10 nucleotide sequences( starting with purine) sigma factor is released & it elongates.

3. Termination: Row dependent RNA folds back on itself, forming GC rich,hairpin structure Row independent Row is requires, it binds C rich near 3 end

4. Action of Antibiotics: Rifampin inhibits (beta subunit) Dectinomycin tumor therapy TRANSCRIPTION IN EUKARYOTES Separate polys + TFs Chromatin structure & gene expression Euchromatin(relaxed) Heterochromatin Acetylation of lysine residues at histones eliminates +ve change RNA polymerase 1 28s,18s,5. 8s of rRNA RNA polymerase 2 mRNA, ncRNA , miRNA RNA polymerase 3 tRNA , 5S , rRNA,sRNA Promoters 25 nucleotide upstream TATA hog-ness 70-80 CAAT CIS acting Gene on same molecule of DNA on which it have work TF 2D recognize & bind TATA box TF2F begins polymerase to promotor TF2H melts DNA Enhancers CIS acting pol 2 silencer Inhibitors Alpha amanitin for RNA Pol2 Mitochondrial RNA pol resembles bacterial poly POST TRANSLATIONAL MODIFICATIONS r RNA: 5 s RNA by poly 3 They are cleaved by ribonucleases Base & sugar modification t RNA

 16 nucleotide cleaved at 5 end by ribozyme 14 nucleotide anticodon removed by nuclease Uracil residues at 3 end replaced by CCA Modified base Note: same changes in eukaryotic & prokaryotic m RNA Note: No changes in prokaryotes Changes in Eukaryotes: 5 terminal, 7 methyl-guanosine cap 5-5 triphosphate linkage, s-adenosyl methionine is source of methyl group,added ny guanyl-transferase by removing phosphate adding GMP Poly A tail, 40-200 adenine nucleotide 3-end,not transcribed,by polyadenylate polymerase, AAUAAA facilitates it to exit from nucleus Removal of introns,splicing by splicosomes,histones have no introns, SnRNA uracil rich helps splicing snRNA binds, 2 OH group of adenosine (branch site) attacks phosphate at 5 end(donor),2-5 linkage forms,lariat forms,3 OH of exon 1 attach 5 phosphate at splice acceptor site Beta thalassemia is error in splicing Systemic lupus lupus erythematosus is fatal inflammatory disease,autoimmune antibodies for snRNAs PROTEIN SNTHYSIS Codons: Genetic words in m RNA are codons 61 codons 20 amino acids 3 codons stop codons UGA= u go away UAA= u are away UAG= u are gone Total 64 codons 1.specificity 2.universality(UGA for tryptophan in mitochondria is exception) 3.degeneracy (met & try have 1 type codon) 4.non overlapping Mutations: 1.Silent: UCAUCU serine 2.Missense: UCA CCA proline 3.Nonsense: UCA UAA stop 4.Other mutations: Trinucleotide repeated expansion(extra copies of amino acids) CAG(glutamine)Huntigton disease neurodegenerative disorders

 Repeated untranslated regions(hyper-methylation) fragile X syndrome,myotonic dystrophy Slice site mutations( beta thallesemia major) Frame shift mutation Cystic fibrosis,phenylation loss on 508th position. CFTR normally functions chloride channel in epithelial cells & it causes sticky secretions in lungs & pancreas COMPONENTS OF TRANSLATION: Amino acids tRNAs (amino acid attachment site at its 3rd end,carboxyl group of amino acid ester linkage with 3 hydroxyl of ribose) Aminoacyl t RNA synthetase (ATPAMP+ 2P) m RNA Functionally competent ribosomes 50s 30s 70s : Prokaryotes 60s 40s 80s : Eukaryotes Large unit catalyzes,small unit binds RIBOSOMAL RNA on ribosomal protein AP & E sites for t RNA on both units A incoming aminoacyl t RNA,it specifies next amino acids P Peptidyl t RNA , chain of amino acids E Exits the ribosomes Cellular location of ribosomes: RER ribosomes Plasma+ER+GM+Lysosomes cytosolic ribosomes Cytosol+mitochondria+nucleus Protein factor GTP 4 high energy bonds 2 from aminoacyl t RNA synthetase 2 from GTP (1 from A site & 1 for translocation) Additional GTP & ATP initiation in eukaryotes Additional GTP for termination in both eukaryote+prokaryote Antiparallel binding b/w codon & anti codon codons 5-3 anticodon 3-5 Wooble hypothesis: By which t RNAs can recognize more than 1 codon for a specific amino acid PROTEIN SNTHYSIS Translated 53 , synthesized from its amino carboxyl A: initiation

All factors assembles, - in eukaryotes ATP+GTP in prokaryotes only GTP - in eukaryotes 10 factors e IF ,in prokaryotes IF1..

Ribosomes recognize AUG by 2 ways: 1. Shine delgarno sequence: In e.coli, purine rich, 6-10 bases upstream to AUG on m RNA near its 5 end 16s of 30s has complementary on r RNA Eukaryotes dont have SD but cap binds 40s & scanning needs ATP by e IF4 2.Initiation Codon e IF-2 GTP + e IF s in eukaryotes helps IF2 GTP in prokaryotes In prokaryotes & mitochondria methionine to t RNA is formylated & acts as carbon donor B. elongation Ribosomes move from 53 of m RNA Elongation factor in pro is : EF-Tu-GTP,EFTs-GTP Elongation factor in eukaryotes is: EF1 alpha GTP, EF1 beta gam Peptidyltransferase is activity of 23s (50s) C. termination 3 of any stop codons in A site in prokaryotes by RF1 (UAA,UAG) & RF2(UAA,UGA) Eukaryotes have only e RF POLYSOME: 1 m RNA + numb of ribosomes Protein targeting: Mitochondriaamphipathic Nuclear basic Out of cells hydrophobic Regulation: e IF-2 : phosphorylated e IF 2 is inactive POST TRANSLATIONAL MODIFICATIONS -co-translational modification = still attached to ribosomes -post-translational modification=after getting de-attached 1.Trimming 2.Covalent modification phosphorylation on OH grop of threonine,serine,tyrosine Glycosylation N type In ER Amide nitro of asparaginine O type In Golgi OH of serine, threonine, tyrosine

. Hydroxylation of proline & lysine Other covalent modification carboxylation on glutamate,biotin to amino group of lysinepyruvate carboxylase,lipids attached ,proteins like histones acetylated 3. Protein foldings 4. Protein degeneration REGULATION OF GENE EXPRESSION OPERONS (tryptophan & lac) Iron metabolism ( These 2 are most important rest of the chapter do from summary & key concepts at alst of the chapter from lipincot) BIOTECHNOLOGY & HUMAN DISEASE Sticky & blunt ends Gene cloning from fig 33.6 DNA libraries(concept) PCR (most imp of this chapter) Fig 33.24 imp regarding summarize techniques And digrams & summary si enough from this chapter

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