Le dogme central

The central dogma states that information encoded in DNA is transferred to RNA, which then directs protein synthesis. This process occurs through two main steps: transcription, where DNA serves as a template to synthesize messenger RNA (mRNA), and translation, where mRNA directs the assembly of amino acids into proteins at the ribosome.

During transcription, DNA serves as a template to synthesize mRNA in the nucleus. The mRNA sequence mirrors the DNA coding strand, except uracil replaces thymidine. In eukaryotes, the primary transcript undergoes processing, including removal of non-coding regions, addition of a 5' cap, and a 3' poly-A tail before export to the cytoplasm.

Codons are groups of three nucleotides in mRNA that bind to complementary sequences on transfer RNA (tRNA) molecules. Each tRNA carries a specific amino acid corresponding to its codon. For example, the codon CCA binds to tRNA carrying proline, while AGC binds to tRNA carrying serine, determining the amino acid sequence in the resulting polypeptide.

Proteins are synthesized from 20 amino acids, but four nucleotides combined in triplets create 64 possible codons. This means multiple codons can specify the same amino acid. For instance, GUU, GUC, GUA, and GUG all code for valine. Redundancy minimizes harmful effects of mutations, particularly at the third nucleotide position.

With few exceptions, most prokaryotic and eukaryotic organisms use the same genetic code for protein synthesis. This universality enables biotechnology advances, such as producing human insulin in bacteria using recombinant DNA technology, where human insulin genes are inserted into bacterial cells for large-scale production.

RNA bridges DNA and protein production because protein synthesis occurs in the cytoplasm, where DNA cannot reach. RNA is synthesized in the nucleus using DNA as a template, then exported to the cytoplasm. This intermediary role was discovered when scientists found that DNA remains in the nucleus while proteins are made outside it.

Polypeptides synthesized during translation are often further processed to become functional proteins. This post-translational modification can include folding, cleavage, and addition of chemical groups, transforming the initial polypeptide chain into its active protein form capable of performing cellular functions and roles.