Chapter 17. Transcription and Translation
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1 TRNSRIPTION DN hapter 17 RN transcript RN PROSSIN YTOPLSM xon NLS RN polymerase RN transcript (pre-) Intron Poly- Poly- mino acid trn minoacyltrn synthetase MINO ID TIVTION P Ribosomal subunits ap rowing polypeptide minoacyl (charged) trn Poly- ap odon TRNSLTION nticodon Ribosome Transcription and Translation RN - bridge between genes and proteins Transcription - synthesis of RN () from DN template Translation - synthesis of a polypeptide, protein from Ribosomes - sites of translation DN RN Protein transcription translation eukaryotes transcription in nucleus translation in cytoplasm Nuclear envelope TRNSRIPTION DN RN PROSSIN Pre- TRNSRIPTION DN TRNSLTION Ribosome TRNSLTION Ribosome Polypeptide Polypeptide (a) Bacterial cell (b) ukaryotic cell 1
2 Figure 17.3 Nuclear envelope TRNSRIPTION DN RN PROSSIN Pre- TRNSRIPTION DN TRNSLTION Ribosome TRNSLTION Ribosome Polypeptide Polypeptide (a) Bacterial cell (b) ukaryotic cell odons: Triplets of Nucleotides genes composed of a series of nonoverlapping, three-nucleotide words (codons) codons transcribed into complementary nonoverlapping translated into a chain of amino acids (polypeptide) DN template strand T T T T T T TRNSRIPTION odon TRNSLTION DN molecule ene 1 ene 2 Why not codons of single nucleotides? or two? Protein Trp Phe ly mino acid Ser ene 3 Figure 17.5 First base ( end of codon) Second base Phe Tyr ys Ser Leu Trp His Leu Pro rg ln sn Ser Ile Thr Lys rg Met or start sp Val la ly lu Third base ( end of codon) 2
3 only one DN strand transcribed: template strand read in to direction each codon codes for one of 20 amino acids DN template strand T DN molecule T T T T T TRNSRIPTION odon TRNSLTION ene 1 ene 2 Protein Trp Phe ly mino acid Ser ene 3 Figure 17.4 volution of the enetic ode shared by nearly all organisms genes from one species can be inserted and expressed in another (a) Tobacco plant expressing a firefly gene (b) Pig expressing a jellyfish gene Figure 17.6 Figure
4 DN RN Protein transcription translation RN complementary to DN template strand thymine (T) replaced by uracil () initiation, elongation, termination Figure Promoter Transcription unit Start point DN RN polymerase 1 Initiation nwound DN Rewound DN Nontemplate strand of DN Template strand of DN RN transcript 2 longation RN transcript 3 Termination ompleted RN transcript Direction of transcription ( downstream ) Initiation RN Polymerase binds to promoter Transcription factors mediate binding of RN polymerase, initiates transcription transcription initiation complex TT box Promoter Transcription unit Start point DN RN polymerase 1 Initiation nwound DN Rewound DN RN transcript RN transcript 2 longation Nontemplate strand of DN Template strand of DN 3 Termination ompleted RN transcript Direction of transcription ( downstream ) 4
5 Figure 17.8 DN T T T T T T T TT box Promoter Transcription factors 1 eukaryotic promoter Start point Nontemplate strand 2 Several transcription factors bind to DN Template strand 3 Transcription initiation complex forms RN polymerase II Transcription factors RN transcript Transcription initiation complex longation of the RN Strand RN polymerase adds to 3 end eukaryotes, 40 nucleotides/sec! gene can be transcribed simultaneously by several RN polymerases T Nontemplate strand of DN RN nucleotides RN polymerase T end T T T T T Newly made RN Direction of transcription Template strand of DN Figure 17.9 RN polymerase Nontemplate strand of DN RN nucleotides T T end T T T T T Newly made RN Direction of transcription Template strand of DN 5
6 Termination of Transcription In bacteria - termination sequence signals release of polymerase; transcript ready for translation In eukaryotes - polyadenylation sequence () signals release of RN poly II farther downstream; result is pre- needing processing before translation P P P alteration of ends and intron removal Protein-coding segment Polyadenylation signal ap TR Start codon codon TR Poly- tail Processing of pre- nds modified cap poly- tail ( s) several functions facilitate the export of to the cytoplasm protect from hydrolytic enzymes help ribosomes attach to the end Protein-coding segment Polyadenylation signal P P P ap TR Start codon codon TR Poly- tail Figure Protein-coding segment Polyadenylation signal P P P ap TR Start codon codon TR Poly- tail 6
7 Split enes and RN Splicing Introns - noncoding regions other coding regions exons eventually expressed RN splicing removes introns and joins exons, creating an molecule with a continuous coding sequence Figure Pre- odon numbers introns intervene xon Intron xon ap exons expressed Intron xon Poly- tail Introns cut out and exons spliced together ap TR oding segment Poly- tail TR Spliceosomes (complex of small nuclear ribonucleoproteins [snrnps]) recognize splice sites and remove introns snrns catalyze pre splicing xon 1 Protein snrn Figure RN transcript (pre-) snrnps Intron xon 2 Other proteins Spliceosome Spliceosome components xon 1 xon 2 ut-out intron 7
8 importance of introns? DN ene xon 1 Intron xon 2 Intron xon 3 Transcription RN processing specific functions not identified Translation Domain 3 Domain 2 Domain 1 Polypeptide possible benefits: allows single gene to encode multiple polypeptides (alternative RN splicing) exon shuffling may result in the evolution of new proteins Figure DN ene xon 1 Intron xon 2 Intron xon 3 Transcription RN processing Translation Domain 3 Domain 2 Domain 1 Polypeptide DN RN Protein transcription translation trn translates to protein occurs at ribosomes 8
9 Figure Polypeptide mino acids Trp Phe Ribosome trn with amino acid attached ly trn nticodon odons The Structure and Function of Transfer RN trn transfer amino acids to growing polypeptide at ribosome carries a specific amino acid on one end anticodon on the other end; the anticodon base-pairs with a complementary codon on mino Polypeptide acids trn with amino acid attached Ribosome Trp Phe odons ly trn nticodon Figure mino acid attachment site mino acid attachment site Hydrogen bonds Hydrogen bonds nticodon (a) Two-dimensional structure nticodon (b) Three-dimensional structure nticodon (c) Symbol used in this book 9
10 ccurate translation requires a correct match between a trn and an amino acid a correct match between the trn anticodon and an codon Second base Wobble - Flexible pairing at the third base of a codon trns might bind to more than one codon First base ( end of codon) Phe Leu Leu Ser Pro Tyr His ln ys sn Ile Thr Lys Met or start sp Val la lu Trp rg Ser rg ly Third base ( end of codon) Figure 17.5 First base ( end of codon) Second base Phe Tyr ys Ser Leu Trp His Leu Pro rg ln sn Ser Ile Thr Lys rg Met or start sp Val la ly lu Third base ( end of codon) Figure minoacyl-trn synthetase (enzyme) mino acid P denosine P P TP P denosine P P i P i P i trn minoacyl-trn synthetase trn mino acid P denosine MP omputer model minoacyl trn ( charged trn ) 10
11 Figure trn molecules rowing polypeptide xit tunnel P Large subunit Small subunit (a) omputer model of functioning ribosome P site (Peptidyl-tRN binding site) site (xit site) P xit tunnel site (minoacyltrn binding site) Large subunit mino end rowing polypeptide Next amino acid to be added to polypeptide chain trn binding site Small subunit (b) Schematic model showing binding sites odons (c) Schematic model with and trn Ribosomes large and small subunits made of rrn and proteins three binding sites for trn site holds trn that carries the next amino acid P site holds trn carrying the growing polypeptide chain site is the exit site P site (Peptidyl-tRN binding site) xit tunnel site (xit site) P site (minoacyltrn binding site) Large subunit binding site Small subunit (b) Schematic model showing binding sites Building a Polypeptide - Translation Initiation longation Termination protein factors aid in process, assemble complexes 11
12 Ribosome ssociation and Initiation of Translation initiation stage - binds with trn carrying first amino acid, and two ribosomal subunits Initiator trn Met Start codon binding site TP Small ribosomal subunit P i + DP P site Met Large ribosomal subunit Translation initiation complex Figure Initiator trn Met Start codon binding site TP Small ribosomal subunit P i + DP P site Met Large ribosomal subunit Translation initiation complex longation of the Polypeptide hain amino acids added one by one to preceding amino acid at -terminus of growing chain 1) codon recognition 2) peptide bond formation 3) translocation mino end of polypeptide Ribosome ready for P site site next aminoacyl trn TP DP + P i Translation proceeds 5 to 3 P DP+ P i TP P P 12
13 Figure mino end of polypeptide Ribosome ready for next aminoacyl trn P site site TP DP + P i P P DP + P i TP P Termination of Translation stop codon in the reaches site of ribosome release factor causes the addition of H 2 O instead of an amino acid releases polypeptide, translation complex disassembles Release factor Free polypeptide 2 TP codon (,, or ) 2 DP+ 2 P i Figure Release factor Free polypeptide 2 TP codon (,, or ) 2 DP + 2 P i 13
14 Polyribosomes multiple ribosomes can translate a single simultaneously advantages? rowing polypeptides ompleted polypeptide Incoming ribosomal subunits Start of ( end) (a) Polyribosome nd of ( end) Ribosomes (b) 0.1 µm Figure rowing polypeptides Incoming ribosomal subunits ompleted polypeptide what happens to complete polypeptide? (a) Start of ( end) Polyribosome nd of ( end) Ribosomes (b) 0.1 µm ompleting and Targeting the Functional Protein chaperone proteins help protein folding 1, 2, 3 structures modifications to amino acids addition of sugars, lipids, phosphate groups removal of amino acids 14
15 Targeting Polypeptides to Specific Locations free ribsomes (in cytosol) and bound ribosomes (attached to R) free ribosomes - proteins in cytosol bound ribosomes - proteins destined to endomembrane system or for secretion out of cell Ribosomes are identical and can switch from free to bound Polypeptide synthesis begins in cytosol finishes in the cytosol unless polypeptide signals the ribosome to attach to the R signal peptide 1 Ribosome SRP R LMN Signal peptide 2 SRP receptor protein Translocation complex Signal peptide removed R membrane Protein 6 YTOSOL Figure Ribosome 4 5 SRP R LMN Signal peptide 2 SRP receptor protein Translocation complex 3 Signal peptide removed R membrane Protein 6 YTOSOL 15
16 Mutations of one or a few nucleotides can affect protein structure and function changes in genetic material point mutations - change one base pair of gene change of single nucleotide can produce abnormal protein Figure Wild-type hemoglobin Wild-type hemoglobin DN Sickle-cell hemoglobin Mutant hemoglobin DN T T T T Normal hemoglobin lu Sickle-cell hemoglobin Val Types of Small-Scale Mutations Nucleotide-pair substitutions One or more nucleotide-pair insertions or deletions DN template strand Protein mino end (a) Nucleotide-pair substitution instead of T T T T T T T T T T T instead of Met Lys Phe ly Silent (no effect on amino acid sequence) Missense T instead of T T T T T T T T T T T instead of Met Lys Phe Ser instead of T T T T T T T T T T T instead of Nonsense Met Wild type T T T T T T T T T T Met Lys Phe ly arboxyl end (b) Nucleotide-pair insertion or deletion xtra T T T T T T T T T T T xtra Met Frameshift causing immediate nonsense (1 nucleotide-pair insertion) Met Lys missing T T T T T T T T T T missing Frameshift causing extensive missense (1 nucleotide-pair deletion) T T missing Leu la T T T T T T T T missing Met Phe ly No frameshift, but one amino acid missing (3 nucleotide-pair deletion) 16
17 Figure Wild type DN template strand T T T T T T T T T T Protein Met Lys Phe ly mino end arboxyl end (a) Nucleotide-pair substitution instead of T T T T T T T T T T T instead of Met Lys Phe ly Silent (no effect on amino acid sequence) (b) Nucleotide-pair insertion or deletion xtra T T T T T T T T T T T xtra Met Frameshift causing immediate nonsense (1 nucleotide-pair insertion) T instead of missing T T T T T T T T T T T T T T T T T T T T T instead of missing Met Lys Phe Ser Met Lys Leu la Missense Frameshift causing extensive missense (1 nucleotide-pair deletion) instead of T T T T T T T T T T T instead of Met Nonsense T T missing T T T T T T T T missing Met Phe ly No frameshift, but one amino acid missing (3 nucleotide-pair deletion) Figure 17.24a Wild type DN template strand T T T T T T T T T T Protein Met Lys Phe ly mino end arboxyl end (a) Nucleotide-pair substitution: silent Met Lys Phe ly instead of T T T T T T T T T T T instead of produces same amino acid WHY? Figure 17.24b Wild type DN template strand T T T T T T T T T T Protein Met Lys Phe ly mino end arboxyl end (a) Nucleotide-pair substitution: missense T instead of T T T T T T T T T T T instead of Met Lys Phe Ser still code for an amino acid, but not correct 17
18 Figure 17.24c Wild type DN template strand T T T T T T T T T T Protein Met Lys Phe ly mino end arboxyl end (a) Nucleotide-pair substitution: nonsense instead of T T T T T T T T T T T instead of Met changes amino acid codon into stop codon protein usually nonfunctional Insertions and Deletions additions or losses of nucleotide pairs in a gene alters reading frame - frameshift mutation often more serious than substitutions Figure 17.24d Wild type DN template strand T T T T T T T T T T Protein mino end Met Lys Phe ly arboxyl end (b) Nucleotide-pair insertion or deletion: frameshift causing immediate nonsense xtra T T T T T T T T T T T xtra Met 1 nucleotide-pair insertion 18
19 Figure 17.24e Wild type DN template strand T T T T T T T T T T Protein mino end Met Lys Phe ly arboxyl end (b) Nucleotide-pair insertion or deletion: frameshift causing extensive missense missing T T T T T T T T T missing Met Lys Leu la 1 nucleotide-pair deletion Figure 17.24f Wild type DN template strand T T T T T T T T T T Protein mino end Met Lys Phe ly arboxyl end (b) Nucleotide-pair insertion or deletion: no frameshift, but one amino acid missing T T missing T T T T T T T T missing Met Phe ly 3 nucleotide-pair deletion Mutagens Spontaneous mutations can occur during DN replication, recombination, or repair Mutagens are physical or chemical agents that can cause mutations 19
20 BI picture concept of a gene is universal transcription, translation very similar in bacteria, eukaryotes differences: in machinery: RN polymerases, transcription termination in location: bacteria lack nuclei Figure RN polymerase DN Polyribosome RN polymerase Direction of transcription 0.25 µm DN Polyribosome Polypeptide (amino end) Ribosome ( end) Figure TRNSRIPTION DN RN transcript RN PROSSIN YTOPLSM xon NLS RN polymerase RN transcript (pre-) Intron Poly- Poly- mino acid trn minoacyltrn synthetase MINO ID TIVTION P Ribosomal subunits ap rowing polypeptide minoacyl (charged) trn Poly- ap odon TRNSLTION nticodon Ribosome 20
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