explain the relationship between genes, proteins and phenotype with respect to the: TYR gene, tyrosinase and albinism, HBB gene, haemoglobin and sickle cell anaemia, F8 gene, factor VIII and haemophilia, HTT gene, huntingtin and Huntington’s disease

Objective

Explain how a gene determines a protein, how mutations alter that protein, and how the resulting change in protein activity produces a specific phenotype. Use the following examples, linking each to its mode of inheritance:

  • TYR → tyrosinase → oculocutaneous albinism (autosomal recessive)
  • HBB → β‑globin → sickle‑cell anaemia (autosomal recessive)
  • F8 → factor VIII → haemophilia A (X‑linked recessive)
  • HTT → huntingtin → Huntington’s disease (autosomal dominant, anticipation)

1. Flow of Genetic Information (Central Dogma)

  1. Gene (DNA) – defined stretch of nucleotides on a chromosome.
  2. Replication – semi‑conservative copying of DNA before cell division.
  3. Transcription – synthesis of a complementary pre‑mRNA by RNA polymerase II.
  4. RNA processing – 5′‑capping, splicing of introns, poly‑A tail addition to give mature mRNA.
  5. Translation – ribosome reads mRNA codons; tRNAs deliver amino‑acids to build a polypeptide.
  6. Post‑translational events – folding (often with chaperones), cleavage, phosphorylation, glycosylation, etc., generate the functional protein.
  7. Phenotype – the observable trait or disease state that results from the protein’s activity (or its loss).

Key Enzymes & Molecular Players

StepMajor Enzyme/ComplexPrincipal Function
DNA unwindingDNA helicase (e.g., MCM complex)Separates the two strands of the double helix.
Leading‑strand synthesisDNA polymerase εAdds nucleotides continuously 5′→3′.
Lagging‑strand synthesisDNA polymerase δ + primaseProduces Okazaki fragments.
Fragment joiningDNA ligase ISeals nicks between Okazaki fragments.
Proofreading & repair3′→5′ exonuclease activity of Pol δ/ε; Mismatch‑repair (MSH, MLH)Corrects mis‑incorporated bases.
Transcription initiationRNA polymerase II + general transcription factors (TFIID, TFIIH)Recognises promoter (TATA box) and begins RNA synthesis.
RNA cappingRNA 5′‑triphosphatase, guanylyltransferase, methyltransferaseAdds 7‑methyl‑G cap.
SplicingSpliceosome (snRNPs U1, U2, U4/5/6)Removes introns, ligates exons.
Poly‑A tailingPoly‑A polymeraseAdds ~200 A residues to 3′ end.
Translation initiationeIFs, 40S & 60S ribosomal subunits, Met‑tRNAiAssembles ribosome at the 5′‑cap.
Elongation & terminationeEFs, release factors (eRF1/eRF3)Adds amino‑acids and releases the polypeptide at stop codons.
Protein folding & modificationChaperones (Hsp70, Hsp90), protein kinases, glycosyltransferasesAssists correct 3‑D structure; adds phosphate, carbohydrate, etc.

2. Types of Mutations and Typical Molecular Consequences

Mutation typeMechanistic effectTypical protein outcomeCambridge‑relevant example
Missense (point)Single‑base substitution changes one codon.Single amino‑acid change; may alter activity, stability or localisation.HBB Glu⁶→Val (sickle‑cell disease)
Nonsense (point)Creates a premature stop codon.Truncated protein; usually non‑functional or degraded.TYR nonsense mutation → OCA1
Frameshift (insertion/deletion)Insertion/deletion not in multiples of three shifts the reading frame.Aberrant amino‑acid sequence downstream; early stop codon.ΔF508 in CFTR (cystic fibrosis – useful for technique comparison)
Repeat expansionIncrease in the number of tandem repeats (e.g., CAG).Extended poly‑glutamine tract → protein misfolding, aggregation.HTT CAG ≥36 repeats → Huntington’s disease
Large‑scale (deletion, duplication, inversion, translocation)Loss or gain of whole exons/genes or rearrangement of chromosome segments.Missing or extra protein domains; dosage effects.Large deletion in F8 → severe haemophilia A
Regulatory / promoter mutationAltered transcription factor binding.Reduced or absent mRNA → little or no protein.Promoter mutation in TYR reduces transcription.
Epigenetic modificationDNA methylation or histone modification without sequence change.Gene silencing or up‑regulation.Hypermethylation of tumour‑suppressor genes in cancer (contextual example).

3. Case Studies – Gene → Protein → Phenotype

3.1 TYR Gene – Tyrosinase – Oculocutaneous Albinism Type 1 (OCA1)

  • Gene: TYR (11q14.3), autosomal recessive.
  • Protein function: Copper‑containing oxidase catalysing:

    1. Tyrosine → DOPA
    2. DOPA → DOPA‑quinone
    These reactions initiate melanin synthesis.
  • Typical mutations: Missense, nonsense, frameshift or promoter lesions that abolish enzyme activity.
  • Effect on protein: Little or no functional tyrosinase → melanin production stops.
  • Phenotype: Pale skin, white hair, light irises, photophobia, reduced visual acuity; inheritance follows a classic 1:4 carrier ratio in families.

3.2 HBB Gene – β‑Globin – Sickle‑Cell Anaemia

  • Gene: HBB (11p15.5), autosomal recessive.
  • Normal protein: β‑globin pairs with two α‑chains to form adult haemoglobin (HbA, α₂β₂) for O₂ transport.
  • Common mutation: A→T transversion in codon 6 (GAG → GTG) → Glu⁶→Val (β⁽ˢ⁾).
  • Effect on protein: Valine creates a hydrophobic patch; de‑oxygenated HbS polymerises, distorting RBCs into a sickle shape.
  • Phenotypic consequences: Chronic haemolytic anaemia, vaso‑occlusive pain crises, splenic infarction, increased infection risk. Homozygotes (ss) are affected; heterozygotes (AS) show carrier advantage against malaria (balanced polymorphism).

3.3 F8 Gene – Factor VIII – Haemophilia A

  • Gene: F8 (Xq28), X‑linked recessive.
  • Protein function: Large glycoprotein co‑factor for factor IXa; together they form the intrinsic tenase complex (VIIIa·IXa) that activates factor X → Xa, leading to thrombin generation and fibrin clot formation.
  • Typical mutations: Large deletions, nonsense mutations, splice‑site changes, or intron‑13 inversion that abolish functional factor VIII.
  • Effect on protein: Factor VIII absent or non‑functional → intrinsic pathway cannot generate sufficient factor Xa.
  • Phenotype: Prolonged activated partial thromboplastin time (aPTT), spontaneous joint haemorrhages, excessive bleeding after minor trauma. Males are affected; carrier females may show mild symptoms due to lyonisation.

3.4 HTT Gene – Huntingtin – Huntington’s Disease

  • Gene: HTT (4p16.3), autosomal dominant with anticipation.
  • Normal protein: Huntingtin – cytoplasmic protein involved in vesicular transport, transcription regulation and mitochondrial function.
  • Mutation type: Expansion of a CAG trinucleotide repeat in exon 1.

    • Normal: 10–35 repeats
    • Pathogenic: ≥36 repeats (often >40)

  • Pathogenic mechanism: Poly‑glutamine tract causes misfolding and intracellular aggregation; aggregates interfere with transcription, mitochondrial respiration and axonal transport, leading to selective loss of medium spiny neurons in the striatum.
  • Phenotype: Progressive chorea, dystonia, cognitive decline, psychiatric disturbance; age of onset inversely correlated with repeat length. Each generation tends to inherit a longer repeat (anticipation).

4. Inheritance Patterns & Population Genetics (Cambridge Topic 16)

4.1 Mendelian Segregation

  • Autosomal recessive (TYR, HBB):

    • Genotype ratios in offspring of two heterozygotes: 1 AA : 2 Aa : 1 aa.
    • Phenotypic ratio: 3 normal : 1 affected.

  • X‑linked recessive (F8):

    • Male genotype: XⁿY (affected) or X⁺Y (normal).

      Female genotype: XⁿXⁿ (affected), XⁿX⁺ (carrier), X⁺X⁺ (normal).

    • Typical pedigree: affected males in every generation, no male‑to‑male transmission.

  • Autosomal dominant with anticipation (HTT):

    • One affected parent transmits the mutant allele to 50 % of children.
    • Repeat expansion during meiosis leads to earlier onset in successive generations.

4.2 Pedigree Analysis Tips (Cambridge Exam)

  • Identify the mode of inheritance by looking for:

    • Sex bias (X‑linked),
    • Vertical transmission (dominant),
    • Horizontal transmission with skipped generations (recessive).

  • Use symbols: squares = male, circles = female, filled = affected, half‑filled = carrier (for X‑linked).
  • Calculate carrier risk: e.g., for an autosomal recessive disorder, two unaffected parents with an affected child each have a 2⁄3 chance of being carriers.

4.3 Hardy–Weinberg Equilibrium (Population Genetics)

For a single‑gene, two‑allele system (p = frequency of normal allele, q = frequency of mutant allele):

  • Genotype frequencies: p² (homozygous normal) + 2pq (heterozygous carriers) + q² (affected).
  • Example – albinism in a population where 1 in 20 000 individuals is affected (q² = 0.00005):

    q ≈ 0.0071, p ≈ 0.9929, carrier frequency ≈ 2pq ≈ 0.014 ≈ 1 in 71.

Use Hardy–Weinberg to predict disease prevalence, carrier rates, and the impact of selection (e.g., sickle‑cell heterozygote advantage in malaria‑endemic regions).

5. Summary Table – Gene → Protein → Mutation → Phenotype → Inheritance

GeneProtein (function)Typical mutationEffect on proteinPhenotypeInheritance pattern
TYRTyrosinase – catalyses first steps of melanin synthesisMissense / nonsense / frameshift / promoter loss‑of‑functionEnzyme activity reduced or absentOculocutaneous albinism type 1 (pale skin, visual defects)Autosomal recessive
HBBβ‑globin – part of adult haemoglobin (O₂ transport)Missense (GAG→GTG) → Glu⁶→ValHbS polymerises under low O₂, distorts RBCsSickle‑cell anaemia (anaemia, pain crises, organ damage)Autosomal recessive (balanced polymorphism in malaria zones)
F8Factor VIII – co‑factor in intrinsic clotting cascadeLarge deletions, nonsense, splice‑site, intron‑13 inversionFactor VIII absent or non‑functionalHaemophilia A (excessive bleeding, joint haemorrhages)X‑linked recessive
HTTHuntingtin – vesicle transport, transcription regulation, mitochondrial supportCAG repeat expansion (≥36 repeats)Poly‑Q tract causes misfolding & aggregationHuntington’s disease (chorea, cognitive decline, psychiatric symptoms)Autosomal dominant with anticipation

6. Key Take‑aways

  • Genes encode proteins; the structure and activity of those proteins determine cellular function and thus the organism’s phenotype.
  • Mutations can alter the amount of protein produced (null alleles, promoter defects) or its structure (missense, nonsense, frameshift, repeat expansion).
  • The phenotypic outcome reflects the normal physiological role of the protein – loss of pigment, altered oxygen transport, impaired clotting, or neurotoxicity.
  • Understanding the gene → protein → phenotype chain is essential for diagnosis, genetic counselling, and the development of targeted therapies (enzyme replacement, gene therapy, small‑molecule modulators).
  • Linking each disorder to its mode of inheritance and to population‑genetics concepts (Hardy–Weinberg, carrier frequency, selection) satisfies Cambridge AS & A Level requirements for Topics 6 and 16.