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Incoming links: RNA replication
The central dogma of molecular biology concerns sequence information: DNA can be copied by DNA replication; transcription makes RNA from DNA; and translation makes a protein from messenger RNA. The familiar DNA→RNA→protein diagram is not an assertion that all information transfer is one-way: reverse transcription and RNA replication are compatible with the dogma. Its key exclusion is transfer of a protein's amino-acid sequence back into nucleic-acid sequence by a general templating mechanism.
DNA is a polymer of deoxyribonucleotides with a sugar–phosphate backbone joined by phosphodiester bonds. Its usual DNA double helix contains antiparallel strands with complementary bases, adenine paired with thymine and guanine with cytosine. The base sequence stores inherited information; complementary pairing supports accurate copying and repair. A strand has distinct 5′ and 3′ ends, and ordinary chain synthesis extends the 3′ end. Packaging into chromosomes compacts and regulates access to the genetic material.
RNA uses ribose, with a 2′ hydroxyl group, and uracil in place of thymine. It is usually single-stranded but forms extensive paired secondary and tertiary structures. Messenger RNA conveys coding information, transfer RNA couples codons to amino acids, and ribosomal RNA provides both structural organization and catalysis within the ribosome. Other RNA molecules regulate expression or catalyse reactions. Thus RNA is not merely a passive intermediate.
Proteins are polypeptides of amino acids linked by peptide bonds, read from an amino terminus to a carboxyl terminus. Their primary sequence guides protein folding; backbone hydrogen bonds organize helices and sheets, while hydrophobic, electrostatic and other interactions produce tertiary and sometimes quaternary protein structure. Their functions include catalysis, transport, signalling, mechanical support and molecular movement. Sequence alone does not guarantee function: folding, modifications, partners and cellular conditions matter. During translation, a ribosome reads successive triplet codons in messenger RNA, with charged transfer RNA molecules supplying the corresponding amino acids; initiation and termination define the reading frame.
Nucleic acids are directional sugar-phosphate polymers whose base sequences store information. Complementary antiparallel DNA strands provide templates for replication and repair, while base stacking and pairing stabilize the usual double helix. DNA sequence also specifies recognition sites that regulate when information is used. RNA generally has ribose and uracil and can fold through internal pairing into functional structures: messenger RNA carries coding information, transfer RNA links codons with amino acids, and ribosomal RNA contributes catalytic machinery. Not all RNA is a passive messenger.
Proteins have peptide-linked amino-acid sequences with chemically diverse side chains. Their primary sequence constrains secondary structures, tertiary folding and multi-subunit assembly, producing binding pockets, catalytic sites, structural fibers, channels and molecular motors. Function depends on conformational dynamics, chemical context and interactions; a linear sequence is not itself a complete account of an active structure. Folding errors and modifications illustrate the need to connect multiple organizational levels.
The central dogma concerns directional transfer of sequence information. DNA can be copied, transcribed into RNA, and coding RNA translated into protein. Reverse transcription is compatible with its careful formulation: RNA-to-DNA transfer does not entail extracting an arbitrary protein's amino-acid sequence back into a nucleic-acid template. RNA replication also occurs. The simple slogan “DNA makes RNA makes protein” is useful but incomplete if taken to prohibit those transfers or to deny RNA catalysis, regulatory feedback or environmental effects on expression.
Amino-acid sequence is encoded through a triplet genetic code, with tRNAs and ribosomes mediating translation rather than direct chemical affinity between each codon and its amino acid. Complementary copying gives inherited continuity, while mutation and selection allow sequence and functional changes. Thus molecular structure supports both stable heredity and adaptable biochemical machinery without making every cellular process a one-way causal chain.[ref]
Molecular Biology of the Cell, 4th edition by Bruce Alberts and others. Chapters 3–6, protein structure, nucleic acids and sequence-information transfer