All you need to know about the course this year (2020)

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Nucleic acids convey genetic information.

AVERY’S BOMBSHELL: DNA CAN CARRY GENETIC SPECIFICITY

Viral Genes Are Also Nucleic Acids

THE DOUBLE HELIX

Chargaff’s Rules

Finding the Polymerases That Make DNA

Experimental Evidence Favors Strand Separation during DNA Replication

THE GENETIC INFORMATION WITHIN DNA IS CONVEYED BY THE SEQUENCE OF ITS FOUR NUCLEOTIDE BUILDING BLOCKS

Evidence That Genes Control Amino Acid Sequences in Proteins

DNA Cannot Be the Template That Directly Orders Amino Acids during Protein Synthesis

RNA Is Chemically Very Similar to DNA

THE CENTRAL DOGMA

The Adaptor Hypothesis of Crick

Discovery of Transfer RNA

The Paradox of the Nonspecific-Appearing Ribosomes

Discovery of Messenger RNA (mRNA)

Enzymatic Synthesis of RNA upon DNATemplates

Establishing the Genetic Code

ESTABLISHING THE DIRECTION OF PROTEIN SYNTHESIS

Start and Stop Signals Are Also Encoded within DNA

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Weak and strong chemical bonds.

CHARACTERISTICS OF CHEMICAL BONDS

Chemical Bonds Are Explainable in Quantum-Mechanical Terms

Chemical-Bond Formation Involves a Change in the Form of Energy

Equilibrium between Bond Making and Breaking

THE CONCEPT OF FREE ENERGY

Keq Is Exponentially Related to DG

Covalent Bonds Are Very Strong

WEAK BONDS IN BIOLOGICAL SYSTEMS

Weak Bonds Have Energies between 1 and 7 kcal/mol

Weak Bonds Are Constantly Made and Broken at Physiological Temperatures

The Distinction between Polar and Nonpolar Molecules

van der Waals Forces

Hydrogen Bonds

Some Ionic Bonds Are Hydrogen Bonds

Weak Interactions Demand Complementary Molecular Surfaces

Water Molecules Form Hydrogen Bonds

Weak Bonds between Molecules in Aqueous Solutions

Organic Molecules That Tend to Form Hydrogen Bonds Are Water Soluble

Hydrophobic “Bonds” Stabilize Macromolecules

ADVANCED CONCEPTS BOX 3-1 The Uniqueness of Molecular Shapes and the Concept of Selective

Stickiness

The Advantage of DG between 2 and 5 kcal/mol

Weak Bonds Attach Enzymes to Substrates

Weak Bonds Mediate Most Protein–DNA and Protein–Protein Interactions

HIGH-ENERGY BONDS

MOLECULES THAT DONATE ENERGY ARE THERMODYNAMICALLY UNSTABLE

ENZYMES LOWER ACTIVATION ENERGIES IN BIOCHEMICAL REACTIONS

FREE ENERGY IN BIOMOLECULES

High-Energy Bonds Hydrolyze with Large Negative ΔG

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The Structure of DNA

DNA STRUCTURE

- DNA Is Composed of Polynucleotide Chains

- Each Base Has Its Preferred Tautomeric Form

- The Two Strands of the Double Helix Are Wound around Each Other in an Antiparallel Orientation

- The Two Chains of the Double Helix Have Complementary Sequences

- The Double Helix Is Stabilized by Base Pairing and Base Stacking

- Hydrogen Bonding Is Important for the Specificity of Base Pairing

- Bases Can Flip Out from the Double Helix

- DNA Is Usually a Right-Handed Double Helix

- DNA Has 10.5 bp per Turn of the Helix in Solution: The Mica Experiment

- The Double Helix Has Minor and Major Grooves

- The Major Groove Is Rich in Chemical Information

- The Double Helix Exists in Multiple Conformations

- DNA Can Sometimes Form a Left-Handed Helix

- How Spots on an X-Ray Film Reveal the Structure of DNA

- DNA Strands Can Separate (Denature) and Reassociate

- Some DNA Molecules Are Circles

DNA TOPOLOGY

- Linking Number Is an Invariant Topological Property of Covalently Closed, Circular DNA

- Topoisomerases Can Relax Supercoiled DNA

- Prokaryotes Have a Special Topoisomerase That Introduces Supercoils into DNA

- Topoisomerases Also Unknot and Disentangle DNA Molecules

- Topoisomerases Use a Covalent Protein–DNA Linkage to Cleave and Rejoin DNA Strands

- Topoisomerases Form an Enzyme Bridge and Pass DNA Segments through Each Other

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The Structure and Versatility of RNA

RNA CONTAINS RIBOSE AND URACIL AND IS USUALLY SINGLE-STRANDED

RNA CHAINS FOLD BACK ON THEMSELVES TO FORM LOCAL REGIONS OF DOUBLE HELIX SIMILAR TO A-FORM DNA

RNA CAN FOLD UP INTO COMPLEX TERTIARY STRUCTURES

NUCLEOTIDE SUBSTITUTIONS IN COMBINATION WITH CHEMICAL PROBING PREDICT RNA STRUCTURE

- An RNA Switch Controls Protein Synthesis by Murine Leukemia Virus

DIRECTED EVOLUTION SELECTS RNAs THAT BIND SMALL MOLECULES

SOME RNAs ARE ENZYMES

- Creating an RNA Mimetic of the Green Fluorescent Protein by Directed Evolution

- he Hammerhead Ribozyme Cleaves RNA by the Formation of a 20, 30 Cyclic Phosphate

- A Ribozyme at the Heart of the Ribosome Acts on a Carbon Center

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The Structure of Proteins

THE BASICS

- Amino Acids

- The Peptide Bond

- Polypeptide Chains

- Three Amino Acids with Special Conformational Properties

- Ramachandran Plot: Permitted Combinations of Main-Chain Torsion Angles f and c

IMPORTANCE OF WATER

PROTEIN STRUCTURE CAN BE DESCRIBED AT FOUR LEVELS PROTEIN DOMAINS

- Polypeptide Chains Typically Fold into One or More Domains

- Basic Lessons from the Study of Protein Structures

- Classes of Protein Domains

- Linkers and Hinges

- Post-Translational Modifications

- The Antibody Molecule as an Illustration of Protein Domains

FROM AMINO-ACID SEQUENCE TO THREE DIMENSIONAL STRUCTURE

- Protein Folding

- Three-Dimensional Structure of a Protein Is Specified by Its Amino Acid Sequence (Anfinsen Experiment)

- Predicting Protein Structure from Amino Acid Sequence

CONFORMATIONAL CHANGES IN PROTEINS

PROTEINS AS AGENTS OF SPECIFIC MOLECULAR RECOGNITION

- Proteins That Recognize DNA Sequence

- Protein–Protein Interfaces

- Proteins That Recognize RNA

ENZYMES: PROTEINS AS CATALYSTS

REGULATION OF PROTEIN ACTIVITY 

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Techniques of Molecular Biology

- NUCLEIC ACIDS: BASIC METHODS

- Gel Electrophoresis Separates DNA and RNA Molecules according to Size

- Restriction Endonucleases Cleave DNA Molecules at Particular Sites

- DNA Hybridization Can Be Used to Identify Specific DNA Molecules

- Hybridization Probes Can Identify Electrophoretically Separated DNAs and RNAs

- Isolation of Specific Segments of DNA

- DNA Cloning

- Vector DNA Can Be Introduced into Host Organisms by Transformation

- Libraries of DNA Molecules Can Be Created by Cloning

- Hybridization Can Be Used to Identify a Specific Clone in a DNA Library

- Chemical Synthesis of Defined DNA Sequences

- The Polymerase Chain Reaction Amplifies DNAs by Repeated Rounds of DNA Replication In Vitro

- Nested Sets of DNA Fragments Reveal Nucleotide Sequences

- Forensics and the Polymerase Chain Reaction

- Shotgun Sequencing a Bacterial Genome

- The Shotgun Strategy Permits a Partial Assembly of Large Genome Sequences

- Sequenators Are Used for High-Throughput Sequencing

- The Paired-End Strategy Permits the Assembly of Large-Genome Scaffolds

- The $1000 Human Genome Is within Reach

GENOMICS

- Bioinformatics Tools Facilitate the Genome-Wide Identification of Protein-Coding Genes

- Whole-Genome Tiling ArraysAreUsed to Visualize the Transcriptome

- Regulatory DNA Sequences Can Be Identified by Using Specialized Alignment Tools

- Genome Editing Is Used to Precisely Alter Complex Genomes

PROTEINS

- Specific ProteinsCanBePurified fromCell Extracts

- Purification of a Protein Requires a Specific Assay

- Preparation of Cell Extracts Containing Active Proteins

- Proteins Can Be Separated from One Another Using Column Chromatography

- Separation of Proteins on Polyacrylamide Gels

- Antibodies Are Used to Visualize Electrophoretically Separated Proteins

- Protein Molecules Can Be Directly Sequenced

PROTEOMICS

- Combining Liquid Chromatography with Mass Spectrometry Identifies Individual Proteins within a Complex Extract

- Proteome Comparisons Identify Important

- Differences between Cells

- Mass Spectrometry Can Also Monitor Protein Modification States

- Protein–Protein Interactions Can Yield Information regarding Protein Function

NUCLEIC ACID–PROTEIN INTERACTIONS

- The Electrophoretic Mobility of DNA Is Altered by Protein Binding

- DNA-Bound Protein Protects the DNA from Nucleases and Chemical Modification

- Chromatin Immunoprecipitation Can Detect Protein Association with DNA in the Cell

- Chromosome Conformation Capture Assays Are Used to Analyze Long-Range Interactions

- In Vitro Selection Can Be Used to Identify a Protein’s DNA- or RNA-Binding Site

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Genome Structure, Chromatin, and the Nucleosome

GENOME SEQUENCE AND CHROMOSOME DIVERSITY

Chromosomes Can Be Circular or Linear

Every Cell Maintains a Characteristic Number of Chromosomes

Genome Size Is Related to the Complexity of the Organism

The E. coli Genome Is Composed Almost Entirely of Genes

More Complex Organisms Have Decreased Gene Density

Genes Make Up Only a Small Proportion of the Eukaryotic Chromosomal DNA

The Majority of Human Intergenic Sequences Are Composed of Repetitive DNA

CHROMOSOME DUPLICATION AND SEGREGATION

Eukaryotic Chromosomes Require Centromeres, Telomeres, and Origins of Replication to Be

Maintained during Cell Division

Eukaryotic Chromosome Duplication and Segregation Occur in Separate Phases of the Cell Cycle

Chromosome Structure Changes as Eukaryotic Cells Divide

Sister-Chromatid Cohesion and Chromosome Condensation Are Mediated by SMC Proteins

Mitosis Maintains the Parental Chromosome Number During Gap Phases, Cells Prepare for the Next Cell Cycle Stage and Check That the Previous Stage Is Completed Correctly

Meiosis Reduces the Parental Chromosome Number

Different Levels of Chromosome Structure Can Be Observed by Microscopy

THE NUCLEOSOME

Nucleosomes Are the Building Blocks of Chromosomes

Histones Are Small, Positively Charged Proteins

The Atomic Structure of the Nucleosome

Histones Bind Characteristic Regions of DNA within the Nucleosome

KEY EXPERIMENTS BOX 8-1 Micrococcal Nuclease and the DNA Associated with the Nucleosome

Many DNA Sequence–Independent Contacts Mediate the Interaction between the Core Histones and

DNA

The Histone Amino-Terminal Tails Stabilize DNA Wrapping around the Octamer

Wrapping of the DNA around the Histone Protein Core Stores Negative Superhelicity

HIGHER-ORDER CHROMATIN STRUCTURE

Heterochromatin and Euchromatin

KEY EXPERIMENTS BOX 8-2 Nucleosomes and Superhelical Densit

Histone H1 Binds to the Linker DNA between Nucleosomes

Nucleosome Arrays Can Form More Complex Structures: The 30-nm Fiber

The Histone Amino-Terminal Tails Are Required for the Formation of the 30-nm Fiber

Further Compaction of DNA Involves Large Loops of Nucleosomal DNA

Histone Variants Alter Nucleosome Function

REGULATION OF CHROMATIN STRUCTURE

The Interaction of DNA with the Histone Octamer Is Dynamic

Nucleosome-Remodeling Complexes Facilitate Nucleosome Movement

Some Nucleosomes Are Found in Specific Positions: Nucleosome Positioning

The Amino-Terminal Tails of the Histones Are Frequently Modified

Protein Domains in Nucleosome-Remodeling and -Modifying Complexes Recognize Modified Histones

KEY EXPERIMENTS

Determining Nucleosome Position in the Cell

Specific Enzymes Are Responsible for Histone Modification

Nucleosome Modification and Remodeling Work Together to Increase DNA Accessibility

NUCLEOSOME ASSEMBLY

Nucleosomes Are Assembled Immediately after DNA Replication

Assembly of Nucleosomes Requires Histone “Chaperones”

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The Replication of DNA

THE CHEMISTRY OF DNA SYNTHESIS

DNA Synthesis Requires Deoxynucleoside Triphosphates and a Primer:Template Junction

DNA Is Synthesized by Extending the 30 End of the Primer

Hydrolysis of Pyrophosphate Is the Driving Force for DNA Synthesis

THE MECHANISM OF DNA POLYMERASE

DNA Polymerases Use a Single Active Site to Catalyze DNA Synthesis

Incorporation Assays Can Be Used to Measure Nucleic Acid and Protein Synthesis

DNA Polymerases Resemble a Hand That Grips the Primer:Template Junction

DNA Polymerases Are Processive Enzymes

Exonucleases Proofread Newly Synthesized DNA

Anticancer and Antiviral Agents Target DNA Replication

THE REPLICATION FORK

Both Strands of DNA Are Synthesized Together at the Replication Fork

The Initiation of a New Strand of DNA Requires an RNA Primer

RNA Primers Must Be Removed to Complete DNA Replication

DNA Helicases Unwind the Double Helix in Advance of the Replication Fork

DNA Helicase Pulls Single-Stranded DNA through a Central Protein Pore

Single-Stranded DNA-Binding Proteins Stabilize ssDNA before Replication

Topoisomerases Remove Supercoils Produced by DNA Unwinding at the Replication Fork

Replication Fork Enzymes Extend the Range of DNA Polymerase Substrates

THE SPECIALIZATION OF DNA POLYMERASES

DNA Polymerases Are Specialized for Different Roles in the Cell

Sliding Clamps Dramatically Increase DNA Polymerase Processivity

Sliding Clamps Are Opened and Placed on DNA by Clamp Loaders

ATP Control of Protein Function: Loading a Sliding Clamp

DNA SYNTHESIS AT THE REPLICATION FORK

Interactions between Replication Fork Proteins Form the E. coli Replisome

INITIATION OF DNA REPLICATION

Specific Genomic DNA Sequences Direct the Initiation of DNA Replication

The Replicon Model of Replication Initiation

Replicator Sequences Include Initiator-Binding Sites and Easily Unwound DNA

The Identification of Origins of Replication and Replicators

BINDING AND UNWINDING: ORIGIN SELECTION AND ACTIVATION BY THE INITIATOR PROTEIN

Protein–Protein and Protein–DNA Interactions Direct the Initiation Process

E. coli DNA Replication Is Regulated by DnaA.ATP Levels and SeqA

Eukaryotic Chromosomes Are Replicated Exactly Once per Cell Cycle

Helicase Loading Is the First Step in the Initiation of Replication in Eukaryotes

Helicase Loading and Activation Are Regulated to Allow Only a Single Round of Replication during Each Cell Cycle

Similarities between Eukaryotic and Prokaryotic DNA Replication Initiation

FINISHING REPLICATION

Type II Topoisomerases Are Required to Separate Daughter DNA Molecules

Lagging-Strand Synthesis Is Unable to Copy the Extreme Ends of Linear Chromosomes

Telomerase Is a Novel DNA Polymerase That Does Not Require an Exogenous Template

Telomerase Solves the End Replication Problem by Extending the 30 End of the Chromosome

Aging, Cancer, and the Telomere Hypothesis

Telomere-Binding Proteins Regulate Telomerase Activity and Telomere Length

Telomere-Binding Proteins Protect Chromosome Ends

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The Mutability and Repair of DNA

REPLICATION ERRORS AND THEIR REPAIR

The Nature of Mutations

Some Replication Errors Escape Proofreading

Expansion of Triple Repeats Causes Disease

Mismatch Repair Removes Errors That Escape Proofreading

DNA DAMAGE

DNA Undergoes Damage Spontaneously from Hydrolysis and Deamination

The Ames Test

DNA Is Damaged by Alkylation, Oxidation, and Radiation

Quantitation of DNA Damage and Its Effects on Cellular Survival and Mutagenesis

Mutations Are Also Caused by Base Analogs and Intercalating Agents

REPAIR AND TOLERANCE OF DNA DAMAGE

Direct Reversal of DNA Damage

Base Excision Repair Enzymes Remove Damaged Bases by a Base-Flipping Mechanism

Nucleotide Excision Repair Enzymes Cleave Damaged DNA on Either Side of the Lesion

Linking Nucleotide Excision Repair and Translesion Synthesis to a Genetic Disorder in Humans

Recombination Repairs DNA Breaks by Retrieving Sequence Information from Undamaged DNA

DSBs in DNA Are Also Repaired by Direct Joining of Broken Ends

Nonhomologous End Joining

Translesion DNA Synthesis Enables Replication to Proceed across DNA Damage

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Mechanisms of Transcription

RNA POLYMERASES AND THE TRANSCRIPTION CYCLE

RNA Polymerases Come in Different Forms but Share Many Features

Transcription by RNA Polymerase Proceeds in a Series of Steps

Transcription Initiation Involves Three Defined Steps

THE TRANSCRIPTION CYCLE IN BACTERIA

Bacterial Promoters Vary in Strength and Sequence but Have Certain Defining Features

Consensus Sequences

The s Factor Mediates Binding of Polymerase to the Promoter

Transition to the Open Complex Involves Structural Changes in RNA Polymerase and in the Promoter DNA

Transcription Is Initiated by RNA Polymerase without the Need for a Primer

During Initial Transcription, RNA Polymerase Remains Stationary and Pulls Downstream DNA into Itself

Promoter Escape Involves Breaking Polymerase–Promoter Interactions and Polymerase Core–s Interactions

The Elongating Polymerase Is a Processive Machine That Synthesizes and Proofreads RNA

The Single-Subunit RNA Polymerases

RNA Polymerase Can Become Arrested and Need Removing

Transcription Is Terminated by Signals within the RNA Sequence

TRANSCRIPTION IN EUKARYOTES

RNA Polymerase II Core Promoters Are Made Up of Combinations of Different Classes of Sequence Element

RNA Polymerase II Forms a Preinitiation Complex with General Transcription Factors at the Promoter

Promoter Escape Requires Phosphorylation of the Polymerase “Tail,"

TBP Binds to and Distorts DNA Using a b Sheet Inserted into the Minor Groove

The Other General Transcription Factors Also Have Specific Roles in Initiation

In Vivo, Transcription Initiation Requires Additional Proteins, Including the Mediator Complex

Mediator Consists of Many Subunits, Some Conserved from Yeast to Human

A New Set of Factors Stimulates Pol II Elongation and RNA Proofreading

Elongating RNA Polymerase Must Deal with Histones in Its Path

Elongating Polymerase Is Associated with a New Set of Protein Factors Required for Various Types of RNA

Processing

Transcription Termination Is Linked to RNA Destruction by a Highly Processive RNase

TRANSCRIPTION BY RNA POLYMERASES I AND III

RNA Pol I and Pol III Recognize Distinct Promoters but Still Require TBP

Pol I Transcribes Just the rRNA Genes

Pol III Promoters Are Found Downstream from the Transcription Start Site

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RNA Splicing

THE CHEMISTRY OF RNA SPLICING

Sequences within the RNA Determine Where Splicing Occurs

The Intron Is Removed in a Form Called a Lariat as the Flanking Exons Are Joined

Adenovirus and the Discovery of Splicing

THE SPLICEOSOME MACHINERY

RNA Splicing Is Performed by a Large Complex Called the Spliceosome

SPLICING PATHWAYS

Assembly, Rearrangements, and Catalysis within the Spliceosome: The Splicing Pathway

Spliceosome Assembly Is Dynamic and Variable and Its Disassembly Ensures That the Splicing Reaction Goes Only Forward in the Cell

Self-Splicing Introns Reveal That RNA Can Catalyze RNA Splicing

Group I Introns Release a Linear Intron Rather Than a Lariat

Converting Group I Introns into Ribozymes

How Does the Spliceosome Find the Splice Sites Reliably?

VARIANTS OF SPLICING

Exons from Different RNA Molecules Can Be Fused by Trans-Splicing

A Small Group of Introns Is Spliced by an Alternative Spliceosome Composed of a Different Set of snRNPs

ALTERNATIVE SPLICING

Single Genes Can Produce Multiple Products by Alternative Splicing

Several Mechanisms Exist to Ensure Mutually Exclusive Splicing

The Curious Case of the Drosophila Dscam Gene: Mutually Exclusive Splicing on a Grand Scale

Mutually Exclusive Splicing of Dscam Exon 6 Cannot Be Accounted for by Any Standard Mechanism and Instead Uses a Novel Strategy

Identification of Docking Site and Selector Sequences

Alternative Splicing Is Regulated by Activators and Repressors

Regulation of Alternative Splicing Determines the Sex of Flies

An Alternative Splicing Switch Lies at the Heart of Pluripotency

EXON SHUFFLING

Exons Are Shuffled by Recombination to Produce Genes Encoding New Proteins

Defects in Pre-mRNA Splicing Cause Human Disease

RNA EDITING

RNA Editing Is AnotherWay of Altering the Sequence of an mRNA

Guide RNAs Direct the Insertion and Deletion of Uridines

Deaminases and HIV

mRNA TRANSPORT

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Translation

MESSENGER RNA

Polypeptide Chains Are Specified by Open Reading Frames

Prokaryotic mRNAs Have a Ribosome-Binding Site That Recruits the Translational Machinery

Eukaryotic mRNAs Are Modified at their 50 and 30 Ends to Facilitate Translation

TRANSFER RNA

tRNAs Are Adaptors between Codons and Amino Acids

CCA-Adding Enzymes: Synthesizing RNA without a Template

tRNAs Share a Common Secondary Structure That Resembles a Cloverleaf

tRNAs Have an L-Shaped Three-Dimensional Structure

ATTACHMENT OF AMINO ACIDS TO tRNA

tRNAs Are Charged by the Attachment of an Amino Acid to the 30-Terminal Adenosine Nucleotide via a High-Energy Acyl Linkage

Aminoacyl-tRNA Synthetases Charge tRNAs in Two Steps

Each Aminoacyl-tRNA Synthetase Attaches a Single Amino Acid to One or More tRNAs

tRNA Synthetases Recognize Unique Structural Features of Cognate tRNAs

Aminoacyl-tRNA Formation Is Very Accurate

Some Aminoacyl-tRNA Synthetases Use an Editing Pocket to Charge tRNAs with High Accuracy

The Ribosome Is Unable to Discriminate between Correctly and Incorrectly Charged tRNAs

THE RIBOSOME

Selenocysteine

The Ribosome Is Composed of a Large and a Small Subunit

The Large and Small Subunits Undergo Association and Dissociation during Each Cycle of Translation

New Amino Acids Are Attached to the Carboxyl Terminus of the Growing Polypeptide Chain

Peptide Bonds Are Formed by Transfer of the Growing Polypeptide Chain from One tRNA to Another

Ribosomal RNAs Are Both Structural and Catalytic Determinants of the Ribosome

The Ribosome Has Three Binding Sites for tRNA

Channels through the Ribosome Allow the mRNA and Growing Polypeptide to Enter and/or Exit the Ribosome

INITIATION OF TRANSLATION

Prokaryotic mRNAs Are Initially Recruited to the Small Subunit by Base Pairing to rRNA

A Specialized tRNA Charged with a Modified Methionine Binds Directly to the Prokaryotic Small Subunit

Three Initiation Factors Direct the Assembly of an Initiation Complex That Contains mRNA and the Initiator tRNA

Eukaryotic Ribosomes Are Recruited to the mRNA by the 50 Cap

Translation Initiation Factors Hold Eukaryotic mRNAs in Circles

uORFs and IRESs: Exceptions That Prove the Rule

The Start Codon Is Found by Scanning Downstream from the 50 End of the mRNA

TRANSLATION ELONGATION

Aminoacyl-tRNAs Are Delivered to the A-Site by Elongation Factor EF-Tu

The Ribosome Uses Multiple Mechanisms to Select against Incorrect Aminoacyl-tRNAs

The Ribosome Is a Ribozyme

Peptide-Bond Formation Initiates Translocation in the Large Subunit

EF-G Drives Translocation by Stabilizing Intermediates in Translocation

EF-Tu–GDP and EF-G–GDP Must Exchange GDP for GTP before Participating in a New Round of Elongation,

A Cycle of Peptide-Bond Formation Consumes Two Molecules of GTP and One Molecule of ATP

TERMINATION OF TRANSLATION

Release Factors Terminate Translation in Response to Stop Codons

Short Regions of Class I Release Factors Recognize Stop Codons and Trigger Release of the Peptidyl Chain

GTP-Binding Proteins

Conformational Switching, and the Fidelity and Ordering of the Events of Translation

GDP/GTP Exchange and GTP Hydrolysis Control the Function of the Class II Release Factor

The Ribosome Recycling Factor Mimics a tRNA

REGULATION OF TRANSLATION

Protein or RNA Binding near the Ribosome-Binding Site Negatively Regulates Bacterial Translation Initiation,

Regulation of Prokaryotic Translation: Ribosomal Proteins Are Translational Repressors of Their Own Synthesis

Antibiotics Arrest Cell Division by Blocking Specific Steps in Translation

Global Regulators of Eukaryotic Translation Target Key Factors Required for mRNA Recognition and Initiator tRNA Ribosome Binding

Spatial Control of Translation by mRNA-Specific 4E-BPs

An Iron-Regulated, RNA-Binding Protein Controls Translation of Ferritin

Translation of the Yeast Transcriptional Activator Gcn4 Is Controlled by Short Upstream ORFs and Ternary Complex Abundance

Ribosome and Polysome Profiling

TRANSLATION-DEPENDENT REGULATION OF mRNA AND PROTEIN STABILITY

The SsrA RNA Rescues Ribosomes That Translate Broken mRNAs

A Frontline Drug in Tuberculosis Therapy Targets SsrA Tagging

Eukaryotic Cells Degrade mRNAs That Are Incomplete or Have Premature Stop Codons

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