A codon table can be used to translate a genetic code into a sequence of amino acids. [1] [2] The standard genetic code is traditionally represented as an RNA codon table, because when proteins are made in a cell by ribosomes, it is messenger RNA (mRNA) that directs protein synthesis. [2] [3] The mRNA sequence is determined by the sequence of genomic DNA. [4] In this context, the standard genetic code is referred to as translation table 1. [3] It can also be represented in a DNA codon table. The DNA codons in such tables occur on the sense DNA strand and are arranged in a 5′-to-3′ direction. Different tables with alternate codons are used depending on the source of the genetic code, such as from a cell nucleus, mitochondrion, plastid, or hydrogenosome. [5]
There are 64 different codons in the genetic code and the below tables; most specify an amino acid. [6] Three sequences, UAG, UGA, and UAA, known as stop codons, [note 1] do not code for an amino acid but instead signal the release of the nascent polypeptide from the ribosome. [7] In the standard code, the sequence AUG—read as methionine—can serve as a start codon and, along with sequences such as an initiation factor, initiates translation. [3] [8] [9] In rare instances, start codons in the standard code may also include GUG or UUG; these codons normally represent valine and leucine, respectively, but as start codons they are translated as methionine or formylmethionine. [3] [9]
The classical table/wheel of the standard genetic code is arbitrarily organized based on codon position 1. Saier, [11] following observations from, [12] showed that reorganizing the wheel based instead on codon position 2 (and reordering from UCAG to UCGA) better arranges the codons by the hydrophobicity of their encoded amino acids. This suggests that early ribosomes read the second codon position most carefully, to control hydrophobicity patterns in protein sequences.
The first table—the standard table—can be used to translate nucleotide triplets into the corresponding amino acid or appropriate signal if it is a start or stop codon. The second table, appropriately called the inverse, does the opposite: it can be used to deduce a possible triplet code if the amino acid is known. As multiple codons can code for the same amino acid, the International Union of Pure and Applied Chemistry's (IUPAC) nucleic acid notation is given in some instances.
Amino-acid biochemical properties | Nonpolar (np) | Polar (p) | Basic (b) | Acidic (a) | Termination: stop codon * | Initiation: possible start codon ⇒ |
1st base | 2nd base | 3rd base | |||||||
---|---|---|---|---|---|---|---|---|---|
U | C | A | G | ||||||
U | UUU | (Phe/F) Phenylalanine (np) | UCU | (Ser/S) Serine (p) | UAU | (Tyr/Y) Tyrosine (p) | UGU | (Cys/C) Cysteine (p) | U |
UUC | UCC | UAC | UGC | C | |||||
UUA | (Leu/L) Leucine (np) | UCA | UAA | Stop (Ochre) * [note 2] | UGA | Stop (Opal) * [note 2] | A | ||
UUG ⇒ | UCG | UAG | Stop (Amber) * [note 2] | UGG | (Trp/W) Tryptophan (np) | G | |||
C | CUU | CCU | (Pro/P) Proline (np) | CAU | (His/H) Histidine (b) | CGU | (Arg/R) Arginine (b) | U | |
CUC | CCC | CAC | CGC | C | |||||
CUA | CCA | CAA | (Gln/Q) Glutamine (p) | CGA | A | ||||
CUG | CCG | CAG | CGG | G | |||||
A | AUU | (Ile/I) Isoleucine (np) | ACU | (Thr/T) Threonine (p) | AAU | (Asn/N) Asparagine (p) | AGU | (Ser/S) Serine (p) | U |
AUC | ACC | AAC | AGC | C | |||||
AUA | ACA | AAA | (Lys/K) Lysine (b) | AGA | (Arg/R) Arginine (b) | A | |||
AUG ⇒ | (Met/M) Methionine (np) | ACG | AAG | AGG | G | ||||
G | GUU | (Val/V) Valine (np) | GCU | (Ala/A) Alanine (np) | GAU | (Asp/D) Aspartic acid (a) | GGU | (Gly/G) Glycine (np) | U |
GUC | GCC | GAC | GGC | C | |||||
GUA | GCA | GAA | (Glu/E) Glutamic acid (a) | GGA | A | ||||
GUG ⇒ | GCG | GAG | GGG | G | |||||
As shown in the above table, NCBI table 1 includes the less-canonical start codons GUG and UUG. [3]
Amino acid | RNA codons | Compressed | Amino acid | RNA codons | Compressed | |
---|---|---|---|---|---|---|
Ala, A | GCU, GCC, GCA, GCG | GCN | Ile, I | AUU, AUC, AUA | AUH | |
Arg, R | CGU, CGC, CGA, CGG; AGA, AGG | CGN, AGR; or CGY, MGR | Leu, L | CUU, CUC, CUA, CUG; UUA, UUG | CUN, UUR; or CUY, YUR | |
Asn, N | AAU, AAC | AAY | Lys, K | AAA, AAG | AAR | |
Asp, D | GAU, GAC | GAY | Met, M | AUG | ||
Asn or Asp, B | AAU, AAC; GAU, GAC | RAY | Phe, F | UUU, UUC | UUY | |
Cys, C | UGU, UGC | UGY | Pro, P | CCU, CCC, CCA, CCG | CCN | |
Gln, Q | CAA, CAG | CAR | Ser, S | UCU, UCC, UCA, UCG; AGU, AGC | UCN, AGY | |
Glu, E | GAA, GAG | GAR | Thr, T | ACU, ACC, ACA, ACG | ACN | |
Gln or Glu, Z | CAA, CAG; GAA, GAG | SAR | Trp, W | UGG | ||
Gly, G | GGU, GGC, GGA, GGG | GGN | Tyr, Y | UAU, UAC | UAY | |
His, H | CAU, CAC | CAY | Val, V | GUU, GUC, GUA, GUG | GUN | |
START | AUG, CUG, UUG | HUG | STOP | UAA, UGA, UAG | URA, UAG; or UGA, UAR |
Amino-acid biochemical properties | Nonpolar (np) | Polar (p) | Basic (b) | Acidic (a) | Termination: stop codon * | Initiation: possible start codon ⇒ |
1st base | 2nd base | 3rd base | |||||||
---|---|---|---|---|---|---|---|---|---|
T | C | A | G | ||||||
T | TTT | (Phe/F) Phenylalanine (np) | TCT | (Ser/S) Serine (p) | TAT | (Tyr/Y) Tyrosine (p) | TGT | (Cys/C) Cysteine (p) | T |
TTC | TCC | TAC | TGC | C | |||||
TTA | (Leu/L) Leucine (np) | TCA | TAA | Stop (Ochre) * [note 2] | TGA | Stop (Opal) * [note 2] | A | ||
TTG ⇒ | TCG | TAG | Stop (Amber) * [note 2] | TGG | (Trp/W) Tryptophan (np) | G | |||
C | CTT | CCT | (Pro/P) Proline (np) | CAT | (His/H) Histidine (b) | CGT | (Arg/R) Arginine (b) | T | |
CTC | CCC | CAC | CGC | C | |||||
CTA | CCA | CAA | (Gln/Q) Glutamine (p) | CGA | A | ||||
CTG | CCG | CAG | CGG | G | |||||
A | ATT | (Ile/I) Isoleucine (np) | ACT | (Thr/T) Threonine (p) | AAT | (Asn/N) Asparagine (p) | AGT | (Ser/S) Serine (p) | T |
ATC | ACC | AAC | AGC | C | |||||
ATA | ACA | AAA | (Lys/K) Lysine (b) | AGA | (Arg/R) Arginine (b) | A | |||
ATG ⇒ | (Met/M) Methionine (np) | ACG | AAG | AGG | G | ||||
G | GTT | (Val/V) Valine (np) | GCT | (Ala/A) Alanine (np) | GAT | (Asp/D) Aspartic acid (a) | GGT | (Gly/G) Glycine (np) | T |
GTC | GCC | GAC | GGC | C | |||||
GTA | GCA | GAA | (Glu/E) Glutamic acid (a) | GGA | A | ||||
GTG ⇒ | GCG | GAG | GGG | G | |||||
Amino acid | DNA codons | Compressed | Amino acid | DNA codons | Compressed | |
---|---|---|---|---|---|---|
Ala, A | GCT, GCC, GCA, GCG | GCN | Ile, I | ATT, ATC, ATA | ATH | |
Arg, R | CGT, CGC, CGA, CGG; AGA, AGG | CGN, AGR; or CGY, MGR | Leu, L | CTT, CTC, CTA, CTG; TTA, TTG | CTN, TTR; or CTY, YTR | |
Asn, N | AAT, AAC | AAY | Lys, K | AAA, AAG | AAR | |
Asp, D | GAT, GAC | GAY | Met, M | ATG | ||
Asn or Asp, B | AAT, AAC; GAT, GAC | RAY | Phe, F | TTT, TTC | TTY | |
Cys, C | TGT, TGC | TGY | Pro, P | CCT, CCC, CCA, CCG | CCN | |
Gln, Q | CAA, CAG | CAR | Ser, S | TCT, TCC, TCA, TCG; AGT, AGC | TCN, AGY | |
Glu, E | GAA, GAG | GAR | Thr, T | ACT, ACC, ACA, ACG | ACN | |
Gln or Glu, Z | CAA, CAG; GAA, GAG | SAR | Trp, W | TGG | ||
Gly, G | GGT, GGC, GGA, GGG | GGN | Tyr, Y | TAT, TAC | TAY | |
His, H | CAT, CAC | CAY | Val, V | GTT, GTC, GTA, GTG | GTN | |
START | ATG, TTG, GTG, CTG [19] | NTG | STOP | TAA, TGA, TAG | TRA, TAR |
The genetic code was once believed to be universal: [20] a codon would code for the same amino acid regardless of the organism or source. However, it is now agreed that the genetic code evolves, [21] resulting in discrepancies in how a codon is translated depending on the genetic source. [20] [21] For example, in 1981, it was discovered that the use of codons AUA, UGA, AGA and AGG by the coding system in mammalian mitochondria differed from the universal code. [20] Stop codons can also be affected: in ciliated protozoa, the universal stop codons UAA and UAG code for glutamine. [21] [note 4] Four novel alternative genetic codes (numbered here 34–37) were discovered in bacterial genomes by Shulgina and Eddy, revealing the first sense codon changes in bacteria. [22] The following table displays these alternative codons.
Amino-acid biochemical properties | Nonpolar (np) | Polar (p) | Basic (b) | Acidic (a) | Termination: stop codon * |
Code | Translation table | DNA codon involved | RNA codon involved | Translation with this code | Standard translation | Notes | ||
---|---|---|---|---|---|---|---|---|
Standard | 1 | Includes translation table 8 (plant chloroplasts). | ||||||
Vertebrate mitochondrial | 2 | AGA | AGA | Stop * | Arg (R) (b) | |||
AGG | AGG | Stop * | Arg (R) (b) | |||||
ATA | AUA | Met (M) (np) | Ile (I) (np) | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Yeast mitochondrial | 3 | ATA | AUA | Met (M) (np) | Ile (I) (np) | |||
CTT | CUU | Thr (T) (p) | Leu (L) (np) | |||||
CTC | CUC | Thr (T) (p) | Leu (L) (np) | |||||
CTA | CUA | Thr (T) (p) | Leu (L) (np) | |||||
CTG | CUG | Thr (T) (p) | Leu (L) (np) | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
CGA | CGA | absent | Arg (R) (b) | |||||
CGC | CGC | absent | Arg (R) (b) | |||||
Mold, protozoan, and coelenterate mitochondrial + Mycoplasma / Spiroplasma | 4 | TGA | UGA | Trp (W) (np) | Stop * | Includes the translation table 7 (kinetoplasts). | ||
Invertebrate mitochondrial | 5 | AGA | AGA | Ser (S) (p) | Arg (R) (b) | |||
AGG | AGG | Ser (S) (p) | Arg (R) (b) | |||||
ATA | AUA | Met (M) (np) | Ile (I) (np) | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Ciliate, dasycladacean and Hexamita nuclear | 6 | TAA | UAA | Gln (Q) (p) | Stop * | |||
TAG | UAG | Gln (Q) (p) | Stop * | |||||
Echinoderm and flatworm mitochondrial | 9 | AAA | AAA | Asn (N) (p) | Lys (K) (b) | |||
AGA | AGA | Ser (S) (p) | Arg (R) (b) | |||||
AGG | AGG | Ser (S) (p) | Arg (R) (b) | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Euplotid nuclear | 10 | TGA | UGA | Cys (C) (p) | Stop * | |||
Bacterial, archaeal and plant plastid | 11 | See translation table 1. | ||||||
Alternative yeast nuclear | 12 | CTG | CUG | Ser (S) (p) | Leu (L) (np) | |||
Ascidian mitochondrial | 13 | AGA | AGA | Gly (G) (np) | Arg (R) (b) | |||
AGG | AGG | Gly (G) (np) | Arg (R) (b) | |||||
ATA | AUA | Met (M) (np) | Ile (I) (np) | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Alternative flatworm mitochondrial | 14 | AAA | AAA | Asn (N) (p) | Lys (K) (b) | |||
AGA | AGA | Ser (S) (p) | Arg (R) (b) | |||||
AGG | AGG | Ser (S) (p) | Arg (R) (b) | |||||
TAA | UAA | Tyr (Y) (p) | Stop * | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Blepharisma nuclear | 15 | TAG | UAG | Gln (Q) (p) | Stop * | As of Nov. 18, 2016: absent from the NCBI update. Similar to translation table 6. | ||
Chlorophycean mitochondrial | 16 | TAG | UAG | Leu (L) (np) | Stop * | |||
Trematode mitochondrial | 21 | TGA | UGA | Trp (W) (np) | Stop * | |||
ATA | AUA | Met (M) (np) | Ile (I) (np) | |||||
AGA | AGA | Ser (S) | Arg (R) (b) | |||||
AGG | AGG | Ser (S) (p) | Arg (R) (b) | |||||
AAA | AAA | Asn (N) (p) | Lys (K) (b) | |||||
Scenedesmus obliquus mitochondrial | 22 | TCA | UCA | Stop * | Ser (S) (p) | |||
TAG | UAG | Leu (L) (np) | Stop * | |||||
Thraustochytrium mitochondrial | 23 | TTA | UUA | Stop * | Leu (L) (np) | Similar to translation table 11. | ||
Pterobranchia mitochondrial | 24 | AGA | AGA | Ser (S) (p) | Arg (R) (b) | |||
AGG | AGG | Lys (K) (b) | Arg (R) (b) | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Candidate division SR1 and Gracilibacteria | 25 | TGA | UGA | Gly (G) (np) | Stop * | |||
Pachysolen tannophilus nuclear | 26 | CTG | CUG | Ala (A) (np) | Leu (L) (np) | |||
Karyorelict nuclear | 27 | TAA | UAA | Gln (Q) (p) | Stop * | |||
TAG | UAG | Gln (Q) (p) | Stop * | |||||
TG | UGA | Stop * | or | Trp (W) (np) | Stop * | |||
Condylostoma nuclear | 28 | TAA | UAA | Stop * | or | Gln (Q) (p) | Stop * | |
TAG | UAG | Stop * | or | Gln (Q) (p) | Stop * | |||
TGA | UGA | Stop * | or | Trp (W) (np) | Stop * | |||
Mesodinium nuclear | 29 | TAA | UAA | Tyr (Y) (p) | Stop * | |||
TAG | UAG | Tyr (Y) (p) | Stop * | |||||
Peritrich nuclear | 30 | TA | UAA | Glu (E) (a) | Stop * | |||
TAG | UAG | Glu (E) (a) | Stop * | |||||
Blastocrithidia nuclear | 31 | TAA | UAA | Stop * | or | Glu (E) (a) | Stop * | |
TAG | UAG | Stop * | or | Glu (E) (a) | Stop * | |||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Cephalodiscidae mitochondrial code | 33 | AGA | AGA | Ser (S) (p) | Arg (R) (b) | Similar to translation table 24. | ||
AGG | AGG | Lys (K) (b) | Arg (R) (b) | |||||
TAA | UAA | Tyr (Y) (p) | Stop * | |||||
TGA | UGA | Trp (W) (np) | Stop * | |||||
Enterosoma [22] | 34 | AGG | AGG | Met (M) (np) | Arg (R) (b) | |||
Peptacetobacter [22] | 35 | CGG | CGG | Gln (Q) (p) | Arg (R) (b) | |||
Anaerococcus and Onthovivens [22] | 36 | CGG | CGG | Trp (W) (np) | Arg (R) (b) | |||
Absconditabacteraceae [22] | 37 | CGA | CGA | Trp (W) (np) | Arg (R) (b) | |||
CGG | CGG | Trp (W) (np) | Arg (R) (b) | |||||
TGA | UGA | Gly (G) (np) | Stop * |
The genetic code is the set of rules used by living cells to translate information encoded within genetic material into proteins. Translation is accomplished by the ribosome, which links proteinogenic amino acids in an order specified by messenger RNA (mRNA), using transfer RNA (tRNA) molecules to carry amino acids and to read the mRNA three nucleotides at a time. The genetic code is highly similar among all organisms and can be expressed in a simple table with 64 entries.
Protein biosynthesis is a core biological process, occurring inside cells, balancing the loss of cellular proteins through the production of new proteins. Proteins perform a number of critical functions as enzymes, structural proteins or hormones. Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences.
In molecular biology, a stop codon is a codon that signals the termination of the translation process of the current protein. Most codons in messenger RNA correspond to the addition of an amino acid to a growing polypeptide chain, which may ultimately become a protein; stop codons signal the termination of this process by binding release factors, which cause the ribosomal subunits to disassociate, releasing the amino acid chain.
The central dogma of molecular biology deals with the flow of genetic information within a biological system. It is often stated as "DNA makes RNA, and RNA makes protein", although this is not its original meaning. It was first stated by Francis Crick in 1957, then published in 1958:
The Central Dogma. This states that once "information" has passed into protein it cannot get out again. In more detail, the transfer of information from nucleic acid to nucleic acid, or from nucleic acid to protein may be possible, but transfer from protein to protein, or from protein to nucleic acid is impossible. Information here means the precise determination of sequence, either of bases in the nucleic acid or of amino acid residues in the protein.
In biology, translation is the process in living cells in which proteins are produced using RNA molecules as templates. The generated protein is a sequence of amino acids. This sequence is determined by the sequence of nucleotides in the RNA. The nucleotides are considered three at a time. Each such triple results in addition of one specific amino acid to the protein being generated. The matching from nucleotide triple to amino acid is called the genetic code. The translation is performed by a large complex of functional RNA and proteins called ribosomes. The entire process is called gene expression.
In molecular biology, a reading frame is a way of dividing the sequence of nucleotides in a nucleic acid molecule into a set of consecutive, non-overlapping triplets. Where these triplets equate to amino acids or stop signals during translation, they are called codons.
A wobble base pair is a pairing between two nucleotides in RNA molecules that does not follow Watson-Crick base pair rules. The four main wobble base pairs are guanine-uracil (G-U), hypoxanthine-uracil (I-U), hypoxanthine-adenine (I-A), and hypoxanthine-cytosine (I-C). In order to maintain consistency of nucleic acid nomenclature, "I" is used for hypoxanthine because hypoxanthine is the nucleobase of inosine; nomenclature otherwise follows the names of nucleobases and their corresponding nucleosides. The thermodynamic stability of a wobble base pair is comparable to that of a Watson-Crick base pair. Wobble base pairs are fundamental in RNA secondary structure and are critical for the proper translation of the genetic code.
A frameshift mutation is a genetic mutation caused by indels of a number of nucleotides in a DNA sequence that is not divisible by three. Due to the triplet nature of gene expression by codons, the insertion or deletion can change the reading frame, resulting in a completely different translation from the original. The earlier in the sequence the deletion or insertion occurs, the more altered the protein. A frameshift mutation is not the same as a single-nucleotide polymorphism in which a nucleotide is replaced, rather than inserted or deleted. A frameshift mutation will in general cause the reading of the codons after the mutation to code for different amino acids. The frameshift mutation will also alter the first stop codon encountered in the sequence. The polypeptide being created could be abnormally short or abnormally long, and will most likely not be functional.
The Nirenberg and Matthaei experiment was a scientific experiment performed in May 1961 by Marshall W. Nirenberg and his post-doctoral fellow, J. Heinrich Matthaei, at the National Institutes of Health (NIH). The experiment deciphered the first of the 64 triplet codons in the genetic code by using nucleic acid homopolymers to translate specific amino acids.
The Nirenberg and Leder experiment was a scientific experiment performed in 1964 by Marshall W. Nirenberg and Philip Leder. The experiment elucidated the triplet nature of the genetic code and allowed the remaining ambiguous codons in the genetic code to be deciphered.
In genetics, a nonsense mutation is a point mutation in a sequence of DNA that results in a nonsense codon, or a premature stop codon in the transcribed mRNA, and leads to a truncated, incomplete, and possibly nonfunctional protein product. Nonsense mutations are not always harmful; the functional effect of a nonsense mutation depends on many aspects, such as the location of the stop codon within the coding DNA. For example, the effect of a nonsense mutation depends on the proximity of the nonsense mutation to the original stop codon, and the degree to which functional subdomains of the protein are affected. As nonsense mutations leads to premature termination of polypeptide chains; they are also called chain termination mutations.
In molecular biology, reading frames are defined as spans of DNA sequence between the start and stop codons. Usually, this is considered within a studied region of a prokaryotic DNA sequence, where only one of the six possible reading frames will be "open". Such an open reading frame (ORF) may contain a start codon and by definition cannot extend beyond a stop codon. That start codon indicates where translation may start. The transcription termination site is located after the ORF, beyond the translation stop codon. If transcription were to cease before the stop codon, an incomplete protein would be made during translation.
Silent mutations, also called synonymous or samesense mutations, are mutations in DNA that do not have an observable effect on the organism's phenotype. The phrase silent mutation is often used interchangeably with the phrase synonymous mutation; however, synonymous mutations are not always silent, nor vice versa. Synonymous mutations can affect transcription, splicing, mRNA transport, and translation, any of which could alter phenotype, rendering the synonymous mutation non-silent. The substrate specificity of the tRNA to the rare codon can affect the timing of translation, and in turn the co-translational folding of the protein. This is reflected in the codon usage bias that is observed in many species. Mutations that cause the altered codon to produce an amino acid with similar functionality are often classified as silent; if the properties of the amino acid are conserved, this mutation does not usually significantly affect protein function.
Xenobiology (XB) is a subfield of synthetic biology, the study of synthesizing and manipulating biological devices and systems. The name "xenobiology" derives from the Greek word xenos, which means "stranger, alien". Xenobiology is a form of biology that is not (yet) familiar to science and is not found in nature. In practice, it describes novel biological systems and biochemistries that differ from the canonical DNA–RNA-20 amino acid system. For example, instead of DNA or RNA, XB explores nucleic acid analogues, termed xeno nucleic acid (XNA) as information carriers. It also focuses on an expanded genetic code and the incorporation of non-proteinogenic amino acids, or “xeno amino acids” into proteins.
The Shine–Dalgarno (SD) sequence is a ribosomal binding site in bacterial and archaeal messenger RNA, generally located around 8 bases upstream of the start codon AUG. The RNA sequence helps recruit the ribosome to the messenger RNA (mRNA) to initiate protein synthesis by aligning the ribosome with the start codon. Once recruited, tRNA may add amino acids in sequence as dictated by the codons, moving downstream from the translational start site.
A synonymous substitution is the evolutionary substitution of one base for another in an exon of a gene coding for a protein, such that the produced amino acid sequence is not modified. This is possible because the genetic code is "degenerate", meaning that some amino acids are coded for by more than one three-base-pair codon; since some of the codons for a given amino acid differ by just one base pair from others coding for the same amino acid, a mutation that replaces the "normal" base by one of the alternatives will result in incorporation of the same amino acid into the growing polypeptide chain when the gene is translated. Synonymous substitutions and mutations affecting noncoding DNA are often considered silent mutations; however, it is not always the case that the mutation is silent.
The start codon is the first codon of a messenger RNA (mRNA) transcript translated by a ribosome. The start codon always codes for methionine in eukaryotes and archaea and a N-formylmethionine (fMet) in bacteria, mitochondria and plastids.
A nonsense suppressor is a factor which can inhibit the effect of the nonsense mutation. Nonsense suppressors can be generally divided into two classes: a) a mutated tRNA which can bind with a termination codon on mRNA; b) a mutation on ribosomes decreasing the effect of a termination codon. It is believed that nonsense suppressors keep a low concentration in the cell and do not disrupt normal translation most of the time. In addition, many genes do not have only one termination codon, and cells commonly use ochre codons as the termination signal, whose nonsense suppressors are usually inefficient.
An expanded genetic code is an artificially modified genetic code in which one or more specific codons have been re-allocated to encode an amino acid that is not among the 22 common naturally-encoded proteinogenic amino acids.
The vertebrate mitochondrial code is the genetic code found in the mitochondria of all vertebrata.