Prokaryotic Gene Regulation and Translation Flashcards

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Comprehensive vocabulary flashcards covering prokaryotic gene regulation, the lac operon, the genetic code, tRNA adapter mechanics, ribosomal structure, translation stages (initiation, elongation, termination), and translational antibiotics.

Last updated 5:46 PM on 10/2/26
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70 Terms

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Operon

A regulatory unit in bacteria consisting of a group of contiguous structural genes under the control of a single promoter, operator, and terminator.

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Polycistronic mRNA

An mRNA molecule that contains the coding sequences for two or more structural genes, allowing coordinated regulation of proteins with a common functional goal.

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lac Operon

An inducible catabolic operon in E. coli that encodes genes required for lactose uptake and metabolism when glucose is absent.

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β\beta-Galactosidase

An enzyme encoded by lacZlacZ that cleaves lactose into glucose and galactose, and converts a small amount of lactose into allolactose.

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Lactose Permease

A membrane transport protein encoded by lacYlacY that is required for the uptake of lactose into the bacterial cell.

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Galactoside Transacetylase

An enzyme encoded by lacAlacA that covalently modifies lactose and related galactoside analogs.

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Allolactose

A small molecule effector and isomer of lactose produced via a side reaction of β\beta-galactosidase that acts as the natural inducer for the lac operon.

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Enzyme Adaptation

The biological phenomenon where a particular enzyme appears in a cell only after the cell has been exposed to that enzyme's substrate.

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François Jacob and Jacques Monod

Researchers who used E. coli to discover the genetic control of enzyme synthesis in operons, earning the 1965 Nobel Prize.

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lacI Gene

A gene located outside the lac operon with its own promoter (ii promoter) that constitutively encodes the lac repressor protein.

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Catabolite Activator Protein (CAP)

An activator protein that binds to the CAP site near the lac promoter when bound to cAMP, enhancing RNA polymerase binding and transcription.

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Cyclic AMP (cAMP)

A small effector molecule synthesized from ATP by adenylyl cyclase whose intracellular levels rise when glucose levels are low.

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Adenylyl Cyclase

The enzyme that converts ATP into cAMP and pyrophosphate, which is inhibited when glucose is transported into the bacterial cell.

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<p>Diauxic Growth</p>

Diauxic Growth

The sequential growth pattern of a bacterium when exposed to two sugars, utilizing the preferred sugar (glucose) first before expressing genes for the second sugar (lactose).

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Operator (lacOlacO)

A regulatory DNA sequence in an operon where a repressor protein binds to inhibit transcription.

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lacI−lacI^- Mutant

A mutant bacterial strain with a defective lacIlacI gene that results in constitutive expression of the lac operon even in the absence of lactose.

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lacZ−lacZ^- Mutant

A mutant bacterial strain that can import lactose via permease but cannot cleave it due to a functional defect in β\beta-galactosidase.

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lacY−lacY^- Mutant

A mutant bacterial strain that cannot import lactose into the cell due to a defect in lactose permease.

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Negative Control

Transcriptional regulation mediated by a repressor protein that inhibits the rate of transcription when bound to DNA.

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Positive Control

Transcriptional regulation mediated by an activator protein that increases the rate of transcription when bound to DNA.

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Inducer

A small effector molecule that increases transcription by either binding an activator to enable DNA binding or binding a repressor to prevent DNA binding.

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Corepressor

A small effector molecule that binds to a repressor protein, causing a conformational change that enables the repressor to bind DNA and inhibit transcription.

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DNA Looping in lac Operon

The structural rearrangement of DNA required for the lac repressor tetramer to bind simultaneously to two operator sites (such as O1O_1 and O2O_2, or O1O_1 and O3O_3).

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Chronic Myeloid Leukemia (CML)

A disease caused by aberrant gene regulation resulting from a reciprocal chromosomal translocation between chromosomes 9 and 22.

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<p>$$BCR::ABL1$$ Fusion Gene</p>

BCR::ABL1BCR::ABL1 Fusion Gene

An oncogenic gene fusion formed by chromosomal translocation that produces a protein with constitutive tyrosine kinase activity stuck in the ON position.

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Archibald Garrod

The physician who first proposed a link between genes and protein production in the early 1900s while studying alkaptonuria ('inborn errors of metabolism').

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Alkaptonuria

An inherited metabolic disorder characterized by black urine and cartilage discoloration caused by a deficiency in homogentisate 1,2-dioxygenase.

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Neurospora crassa

Common bread mold used by Beadle and Tatum to isolate nutritional mutants following X-ray exposure.

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<p>One Gene–One Enzyme Hypothesis</p>

One Gene–One Enzyme Hypothesis

The hypothesis formulated by Beadle and Tatum stating that a single gene directly specifies the production of a specific enzyme in a metabolic pathway.

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Sense Codons

Nucleotide triplets in mRNA that encode specific amino acids within a polypeptide chain.

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Synonymous Codons

Different codons in the genetic code that specify the exact same amino acid.

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Degenerate Code

The property of the genetic code where multiple distinct codons can specify a single amino acid.

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Start Codon

The codon AUG that defines the reading frame for translation and specifies methionine (or formylmethionine in bacteria).

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Stop Codons

The three codons UAA, UAG, and UGA that signal the termination of translation and do not code for any amino acid.

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Adapter Hypothesis

Francis Crick's proposal predicting that a small intermediary molecule (tRNA) recognizes mRNA codons while carrying corresponding amino acids.

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Cell-Free Translation System

An in vitro experimental mixture containing ribosomes, tRNAs, amino acids, and enzymes used by Nirenberg and Matthaei to decipher the genetic code.

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Amino Acid Core Structure

A central carbon atom attached to a hydrogen atom, an amino group (−NH2-\text{NH}_2), a carboxyl group (−COOH-\text{COOH}), and a variable side chain (RR-group).

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RR-group (Side Chain)

The variable chemical structure attached to the central carbon of an amino acid that determines its specific chemical properties (polar, nonpolar, acidic, or basic).

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Peptide Bond

A covalent bond formed between the carboxyl group of one amino acid and the amino group of another via a dehydration synthesis reaction.

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Primary Protein Structure

The linear sequence of amino acids in a polypeptide chain determined directly by DNA coding and linked by peptide bonds.

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Secondary Protein Structure

Regular, localized folding structures (α\alpha-helices and β\beta-pleated sheets) stabilized by hydrogen bonds along the peptide-bonded backbone.

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Tertiary Protein Structure

The overall three-dimensional folded conformation of a single polypeptide chain, stabilized by interactions among RR-groups and the backbone.

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Quaternary Protein Structure

The spatial arrangement and association of two or more individual polypeptide subunits into a multi-subunit protein complex.

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Hemoglobin

A transport protein with quaternary structure consisting of four polypeptide subunits (2 α2\,\alpha-globin and 2 β2\,\beta-globin chains) that each contain a heme group.

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<p>Transfer RNA (tRNA)</p>

Transfer RNA (tRNA)

An adapter RNA molecule displaying a cloverleaf secondary structure that matches mRNA codons with their corresponding amino acids during protein synthesis.

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Acceptor Stem

The stem region of a tRNA molecule ending in a 3′3' single-stranded overhang where an amino acid covalently attaches.

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CCA Sequence

The universal sequence present at the 3′3' end of all mature tRNAs that serves as the site for covalent amino-acid attachment.

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Anticodon Loop

A loop structure in tRNA containing a three-nucleotide sequence complementary to a specific codon on an mRNA strand.

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Inosine

A modified base (I) found in the anticodon of certain tRNAs that can base-pair with U, C, or A at the wobble position.

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Wobble Hypothesis

Francis Crick's 1966 proposal stating that strict Watson-Crick pairing occurs at the first two codon positions, while non-standard pairing can occur at the third codon position.

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Aminoacyl-tRNA Synthetase

One of 20 specific enzymes responsible for covalently attaching the correct amino acid to its corresponding tRNA 3′3' end using ATP.

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Charged tRNA

A transfer RNA molecule covalently bound to its specific amino acid at its 3′3' acceptor stem (also termed aminoacyl-tRNA).

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Bacterial Ribosome (70S)

A prokaryotic translational complex (70S70\text{S}) composed of a 30S30\text{S} small subunit (16S16\text{S} rRNA + 21 proteins) and a 50S50\text{S} large subunit (5S5\text{S} and 23S23\text{S} rRNAs + 34 proteins).

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Eukaryotic Ribosome (80S)

A eukaryotic translational complex (80S80\text{S}) composed of a 40S40\text{S} small subunit (18S18\text{S} rRNA + 33 proteins) and a 60S60\text{S} large subunit (5S5\text{S}, 5.8S5.8\text{S}, and 28S28\text{S} rRNAs + 49 proteins).

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Nucleolus

The eukaryotic nuclear subdomain where rRNA genes are transcribed, processed, and assembled with imported ribosomal proteins into pre-ribosomal subunits.

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<p>A Site (Aminoacyl Site)</p>

A Site (Aminoacyl Site)

The functional site on a ribosome where incoming charged aminoacyl-tRNA molecules bind during translation elongation.

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P Site (Peptidyl Site)

The functional site on a ribosome that holds the tRNA attached to the growing polypeptide chain.

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E Site (Exit Site)

The functional site on a ribosome where uncharged tRNAs move prior to being discharged from the ribosome.

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Shine-Dalgarno Sequence

A purine-rich ribosomal-binding site in bacterial mRNA upstream of the start codon that is complementary to a segment of 16S16\text{S} rRNA in the 30S30\text{S} subunit.

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Initiation Factor 2 (IF2)

A bacterial initiation protein bound to GTP that promotes the binding of the initiator tRNAfMet\text{tRNA}^{\text{fMet}} to the start codon in the P site.

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7-Methylguanosine (m7Gm^7G) Cap

A modified structure at the 5′5' end of eukaryotic mRNA recognized by eIF4 to facilitate small ribosomal subunit binding.

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Kozak's Rules

Sequence rules surrounding the AUG start codon in eukaryotic mRNA that determine optimal start-codon selection during 5′UTR5'\text{UTR} scanning.

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Elongation Factor Tu (EF-Tu)

A bacterial elongation factor that uses GTP hydrolysis to deliver charged aminoacyl-tRNAs to the ribosomal A site.

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Elongation Factor G (EF-G)

A bacterial elongation factor that uses GTP hydrolysis to drive ribosome translocation along mRNA by one codon toward the 3′3' end.

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Peptidyl Transferase

A ribozyme catalytic activity located within the large ribosomal subunit (23S23\text{S} rRNA in bacteria) that forms peptide bonds between amino acids.

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Release Factors RF1 and RF2

Bacterial proteins that recognize stop codons in the A site (RF1 recognizes UAA/UAG; RF2 recognizes UAA/UGA) and promote polypeptide cleavage.

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Polyribosome (Polysome)

A complex formed when multiple ribosomes simultaneously translate a single mRNA molecule, increasing the overall efficiency of protein synthesis.

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Translation Coupling

The simultaneous occurrence of transcription and translation on an mRNA strand in bacteria due to the lack of a nuclear membrane.

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Chloramphenicol

An antibiotic that blocks bacterial translation elongation by acting as a competitive inhibitor of the peptidyl transferase complex.

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Puromycin

An antibiotic that binds to the ribosomal A site and causes premature polypeptide termination, producing shorter proteins.