A= 93+ B = 81-85 C= 60-69 A- = 88-92 B- = 76-80 C- = 50-59 B+ = 86-88 C+ = 69-75Figure 32-8 Base sequence of yeast tRNAAla drawn in the cloverleaf form.Slide 3Figure 32-10 A selection of the modified nucleosides that occur in tRNAs together with their standard abbreviations.Figure 32-10 (continued) A selection of the modified nucleosides that occur in tRNAs together with their standard abbreviations.Table 32-5 Allowed Wobble Pairing Combinations in the Third Codon–Anticodon Position.mRNA/tRNA binding is antiparallelSlide 8Figure 32-64b Ribosomal decoding site. (b) The X-ray structures of T. thermophilus 30S subunit in its complex with U6 and the 17-nt anticodon stem–loop of tRNAPhe.Figure 32-5 The three potential reading frames of an mRNA. Each reading frame would yield a different polypeptide.Figure 32-11b Structure of yeast tRNAPhe. (b) The X-ray structure drawn to show how its base paired stems are arranged form the L-shaped molecule.Figure 32-12 Tertiary base pairing interactions in yeast tRNAPhe.Figure 32-13 An Aminoacyl–tRNA.Figure 32-14 Major identity elements in four tRNAs.Figure 32-17a X-Ray structure of E. coli GlnRS · tRNAGln · ATP. (a) tRNA and ATP wireframe; tRNA sugar–phosphates green, bases magenta, ATP red.Slide 16Slide 17Slide 18Table 32-7 Components of E. coli Ribosomes.Figure 32-76 Reactions involved in the attachment of ubiquitin to a protein.Figure 32-27a Secondary structures of the E. coli ribosomal RNAs. (a) 16S RNA.Figure 32-30 Assembly map of the E. coli small subunit.Slide 23Slide 24Slide 25Slide 26Slide 27Figure 32-31 Cryoelectron microscopy–based image of the E. coli ribosome at ~25 Å resolution.Table 32-10 Some Ribosomal Inhibitors.Figure 32-65 Selection of antibiotics that act as translational inhibitors.Table 32-9 The Soluble Protein Factors of E. coli Protein Synthesis.Figure 32-45 Translational initiation pathway in E. coli.Slide 33Figure 32-43 Some translational initiation sequences recognized by E. coli ribosomes.Slide 35Figure 32-39 Demonstration that polypeptide synthesis proceeds from the N-terminus to the C-terminus.Figure 32-41 Ribosomal peptidyl transferase reaction forming a peptide bond.Figure 32-52 Puromycin.Figure 32-53 Ribosomal tetrahedral intermediate and its analog. (a) Tetrahedral intermediate (red C). (b) CCdA-p-Puro. Tetrahedral phosphoryl group (red P).Slide 40Figure 32-36 Ribosomal subunits in the X-ray structure of the T. thermophilus 70S ribosome in complex with three tRNAs and an mRNA.Figure 32-54 Proposed mechanism of ribosomal peptide synthesis.Figure 32-48 Elongation cycle in E. coli ribosomes. The E site, to which discharged tRNAs are transferred before being released into solution, is not shown.Slide 44Figure 32-58 Ribosomal binding states in the elongation cycle. Note how this scheme elaborates the classical elongation cycle diagrammed in Fig. 32-48.Figure 32-60 Termination pathway in E. coli ribosomes. RF-1 recognizes the Stop codons UAA and UAG, whereas RF-2 (not shown) recognizes UAA and UGA.Figure 32-61 Ribosome-catalyzed hydrolysis of peptidyl–tRNA to form a polypeptide and free tRNA.Slide 48Slide 49Slide 50Slide 51Slide 52Slide 53Slide 54Slide 55Slide 56Slide 57Slide 58Slide 59Table 32-12 Half-lives of Cytoplasmic Enzymes as a Function of Their N-Terminal Residues.Slide 61Slide 62Slide 63Slide 64Slide 65Slide 66Slide 67Slide 68Slide 69Slide 70Slide 71Slide 72Slide 73Slide 74Slide 75Slide 76Slide 77A= 93+ B = 81-85 C= 60-69A- = 88-92 B- = 76-80 C- = 50-59B+ = 86-88 C+ = 69-75Average = 78.4Standard Deviation = 10.6Figure 32-8 Base sequence of yeast tRNAAla drawn in the cloverleaf form.Figure 32-9 Cloverleaf secondary structure of tRNA.Page 1299Figure 32-16Experimentally observed identity elements of RNAs.Figure 32-10 A selection of the modified nucleosides that occur in tRNAs together with their standard abbreviations.Page 1294Figure 32-10 (continued) A selection of the modified nucleosides that occur in tRNAs together with their standard abbreviations.Page 1294Table 32-5 Allowed Wobble Pairing Combinations in the Third Codon–Anticodon Position.Page 1308mRNA/tRNA binding is antiparallel•5’5’3’mRNAtRNACCA-amino acid (3’end)5’endCodon: 1 2 3Anticodon 3 2 1Anticodon 3’---UUG----5’ Codon 5’----CCU----3’Wobble basePage 1338The 30S Subunit P Site(A) Stereo diagram showing details of interactions between 16S rRNA and the codon-anticodon helix.(B) Interactions between the anticodon stem and the ribosome.(C) Electron density map of the 30S P site (composite omit map contoured at 2.0σ) showing the codon (yellow), anticodon (orange), and surrounding features of 16S rRNA (cyan).Korostelev et al. (2006) Cell 126(6): 1065-1077Figure 32-64b Ribosomal decoding site. (b) The X-ray structures of T. thermophilus 30S subunit in its complex with U6 and the 17-nt anticodon stem–loop of tRNAPhe.Figure 32-5 The three potential reading frames of an mRNA. Each reading frame would yield a different polypeptide.Page 1289Figure 32-11b Structure of yeast tRNAPhe. (b) The X-ray structure drawn to show how its base paired stems are arranged form the L-shaped molecule.Page 1295Figure 32-12 Tertiary base pairing interactions in yeast tRNAPhe.Page 1296Figure 32-13 An Aminoacyl–tRNA.Page 1297Figure 32-14 Major identity elements in four tRNAs.Page 1299Figure 32-17aX-Ray structure of E. coli GlnRS · tRNAGln · ATP. (a) tRNA and ATP wireframe; tRNA sugar–phosphates green, bases magenta, ATP red.Page 1300ActivationPage 1311Figure 32-28 Two-dimensional gel electrophoretogram of E. coli small ribosomal subunit proteins.Table 32-7Components of E. coli Ribosomes.Page 1310Figure 32-76 Reactions involved in the attachment of ubiquitin to a protein.Figure 32-27a Secondary structures of the E. coli ribosomal RNAs. (a) 16S RNA. Page 1311Figure 32-30 Assembly map of the E. coli small subunit.Assembly of 30Ssubunit.Model from 0.9 Å x-ray data.Interactions basedon x-linkingFigure 32-31 Cryoelectron microscopy–based image of the E. coli ribosome at ~25 Å resolution.Page 1313Table 32-10 Some Ribosomal Inhibitors.Page 1339Figure 32-65Selection of antibiotics that act as translational inhibitors.Page 1340Table 32-9 The Soluble Protein Factors of E. coli Protein Synthesis.Figure 32-45 Translational initiation pathway in E. coli.Figure 32-43 Some translational initiation sequences recognized by E. coli ribosomes.SD=Shine-Dalgarno sequence complimentaryto rRNA L10Figure 32-39 Demonstration that