Ribonucleic acid (RNA)

Nucleic acid strands align anti-parallelly; therefore, the 5'-AUG-3' codon pairs with the 3'-UAC-5' (or 5'-CAU-3') anticodon.

Transcription produces an RNA strand complementary and anti-parallel to the DNA template strand, replacing thymine with uracil.

The chemical reactivity of the 2'-OH group allows RNA to participate in catalytic mechanisms, giving rise to ribozymes.

The 23S rRNA located in the large (50S) prokaryotic ribosomal subunit acts as the peptidyl transferase ribozyme.

RNA viruses possessing RNA-dependent RNA polymerase can replicate their RNA directly from an RNA template without creating a DNA intermediate.

Alpha-amanitin, a toxin from the death cap mushroom, is a highly specific inhibitor of eukaryotic RNA Polymerase II.

A nonsense mutation converts an amino acid-specifying codon into a termination codon (UAA, UAG, or UGA), shortening the final protein.

Rho factor is an ATP-dependent helicase that tracks along the growing RNA transcript to unwind the RNA-DNA hybrid and terminate transcription.

Transcription initiation begins with a nucleoside triphosphate without clearing the pyrophosphate, leaving a 5'-triphosphate terminal.

Being single-stranded without a permanent complementary partner allows mRNA to remain dynamic and easily accessible to ribosomes.

The transcription bubble is the localized region of single-stranded DNA where RNA polymerase matches incoming ribonucleotides to the template.

In mammals and high eukaryotes, a single large 45S pre-rRNA transcript is synthesized and then cleaved to produce the 18S, 5.8S, and 28S rRNAs.

Accurate translation relies entirely on the precise hydrogen-bond pairing between three consecutive mRNA bases and three complementary tRNA bases.

The T$psi$C loop contains ribothymidine and pseudouridine, which are critical for anchoring the tRNA molecule to the large ribosomal subunit.

Eukaryotic RNA Polymerase III handles the transcription of smaller, structural non-coding RNAs including tRNA and 5S rRNA.

snRNAs combine with specific proteins to form snRNPs ("snurps"), which build the spliceosome machinery responsible for removing introns.

The 2' -OH group acts as a nucleophile that can attack the adjacent phosphodiester backbone, making RNA chemically less stable than DNA.

The Shine-Dalgarno sequence is a purine-rich region upstream of the start codon that pairs with the 16S rRNA of the prokaryotic ribosome.

Transfer RNA bridges the gap by binding to a specific mRNA codon on one end while carrying the corresponding amino acid on the other.