BIOLOGY GLOSSARY

Mutation

A heritable change in the nucleotide sequence of DNA. Mutations range from a single base substitution to large chromosomal rearrangements. They are the ultimate source of all genetic variation — and therefore the raw material of evolution.

01 · Classification

Types of mutation

Type Change Typical effect Example
Substitution (transition) A↔G or C↔T Often synonymous (same amino acid) or missense (different AA). Nonsense if new codon is stop. Sickle cell: A→T gives Glu→Val in HbS
Substitution (transversion) Purine↔Pyrimidine (A↔C, A↔T, G↔C, G↔T) Higher chance of missense due to different base class Many cancer-associated mutations
Insertion (in-frame) +3, +6, … bases One or more extra amino acids inserted; protein may still function Some Duchenne → Becker muscular dystrophy
Insertion (frameshift) +1, +2, +4, +5 … bases All downstream codons change; usually truncated or non-functional protein Most CRISPR NHEJ outcomes
Deletion (in-frame) −3, −6, … bases One or more amino acids missing; depends on domain importance 3-bp CFTR ΔF508 deletion
Deletion (frameshift) −1, −2, −4, −5 … bases Same as frameshift insertion — devastating downstream Many loss-of-function disease mutations
Chromosomal deletion Large segment removed Multiple genes lost; often lethal in homozygote DiGeorge syndrome (22q11 deletion)
Chromosomal duplication Segment duplicated Extra gene copies; may increase protein expression Charcot-Marie-Tooth disease (PMP22 duplication)

Substitution terminology

A substitution that changes an amino acid is a missense mutation. One that creates a premature stop codon is nonsense. One that changes the codon but not the amino acid (due to codon redundancy) is synonymous or silent. The codon table has 64 entries for 20 amino acids plus 3 stop signals — this redundancy buffers the genome against some substitutions. See Protein synthesis for the full codon table.

02 · Causes

How mutations arise

Replication errors

DNA polymerase adds the wrong base approximately once every 10⁷–10⁸ base pairs during replication. Proofreading (3′→5′ exonuclease activity) reduces this to ~1 in 10⁹. Mismatch repair lowers the final error rate to approximately 1 in 10¹⁰. For the human genome (3.2 × 10⁹ bp), this means roughly 1–2 new mutations per cell division — still enough to matter over a lifetime of ~10¹⁶ cell divisions.

Mutagens

  • UV radiation (254 nm) — causes adjacent thymine bases to covalently bond (thymine dimers), distorting the helix and stalling replication. Nucleotide excision repair (NER) removes them; failure causes xeroderma pigmentosum.
  • Ionising radiation (X-rays, gamma, alpha) — causes single- and double-strand breaks. Double-strand breaks are repaired by NHEJ (error-prone) or HDR (accurate but slower).
  • Alkylating agents (e.g. mustard gas, some chemotherapy drugs) — add alkyl groups to bases, causing mispairing during replication.
  • Base analogues (e.g. 5-bromouracil) — are incorporated in place of a normal base and pair with the wrong partner, causing substitutions.
  • Intercalating agents (e.g. ethidium bromide, acridine dyes) — wedge between base pairs, causing insertions or deletions during replication.

03 · Consequences

How mutations change proteins — and phenotypes

The effect of a mutation on phenotype depends on: where in the gene it occurs, what change it makes to the amino acid sequence, and whether the affected amino acid is in a functionally critical region of the protein (active site, structural domain, binding interface).

SICKLE CELL

A → T substitution at codon 6 of beta-globin. Glu (hydrophilic) → Val (hydrophobic). Under low O₂, HbS polymerises → sickle shape → haemolytic anaemia. Heterozygotes gain malaria resistance.

CYSTIC FIBROSIS

ΔF508: 3-bp deletion removes phenylalanine 508 from CFTR. Protein misfolds, is degraded in ER, and never reaches the membrane. Results in viscous mucus in airways and pancreatic ducts.

PROGERIA

G608G in LMNA: a synonymous substitution activates a cryptic splice site, producing a truncated lamin A (progerin) that destabilises the nuclear envelope. CRISPR base editing corrects this in preclinical trials.

CANCER DRIVER

G12V in KRAS: Gly → Val locks the GTPase in active state, driving continuous cell proliferation. Present in ~25 % of all cancers. A major target for new small-molecule inhibitors.

Not all mutations affect function directly. A mutation in a regulatory region can increase or decrease gene expression without changing the protein sequence at all. Copy-number variations (CNVs) duplicate or delete entire stretches of chromosome, changing gene dosage.

04 · Evolution

Mutation as the engine of evolution

Without mutation, there would be no heritable variation; without variation, natural selection has nothing to act on. Mutations create new alleles. Natural selection retains alleles that improve survival and reproduction, removes those that reduce it, and is indifferent to neutral variants. Over many generations and populations, this process drives evolution.

The molecular clock uses the steady rate of neutral substitutions to estimate when two species diverged. Synonymous (silent) substitutions accumulate at an approximately constant rate because they are not under selective pressure — this provides a molecular timescale independent of the fossil record.

CRISPR technology is allowing researchers to correct pathogenic mutations with unprecedented precision. Base editors and prime editors can make single-letter corrections without double-strand breaks, dramatically reducing off-target effects. See CRISPR base editing for the latest clinical applications.

Mutation — common questions

Most mutations are neutral. Synonymous substitutions change the codon but not the amino acid (due to codon redundancy). Mutations in non-coding DNA are often silent. Beneficial mutations — such as the heterozygote advantage of HbS against malaria — can be favoured by natural selection.

From mutation to trait

The Genetics and Inheritance guide shows how new alleles (created by mutation) combine and segregate across generations — from Mendel's pea plants to Hardy–Weinberg equilibrium.

Genetics guide →