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Ribosomes are a kind of enzyme, called ribozymes because the catalytic peptidyl transferase activity that links amino acids together is performed by the ribosomal RNA. [5] In eukaryotic cells, ribosomes are often associated with the intracellular membranes that make up the rough endoplasmic reticulum.
Initial structures of eukaryotic ribosomes were determined by electron microscopy. First 3D structures were obtained at 30–40 Å resolution for yeast [5] and mammalian ribosomes. [6] [7] Higher resolution structures of the yeast ribosome by cryo-electron microscopy allowed the identification of protein and RNA structural elements. [8]
The ribosome of E. coli has about 22 proteins in the small subunit (labelled S1 to S22) and 33 proteins in the large subunit (somewhat counter-intuitively called L1 to L36). All of them are different with three exceptions: one protein is found in both subunits (S20 and L26), [ dubious – discuss ] L7 and L12 are acetylated and methylated forms ...
Ribosomes are the macromolecular machines that are responsible for mRNA translation into proteins. The eukaryotic ribosome, also called the 80S ribosome, is made up of two subunits – the large 60S subunit (which contains the 25S [in plants] or 28S [in mammals], 5.8S, and 5S rRNA and 46 ribosomal proteins) and a small 40S subunit (which contains the 18S rRNA and 33 ribosomal proteins). [6]
It is best known as the site of ribosome biogenesis. The nucleolus also participates in the formation of signal recognition particles and plays a role in the cell's response to stress. [2] Nucleoli are made of proteins, DNA and RNA, and form around specific chromosomal regions called nucleolar organizing regions.
The ribosome catalyzes ester-amide exchange, transferring the C-terminus of a nascent peptide from a tRNA to the amine of an amino acid. These processes are able to occur due to sites within the ribosome in which these molecules can bind, formed by the rRNA stem-loops. A ribosome has three of these binding sites called the A, P and E sites:
Eukaryotic ribosomes are known to bind to transcripts in a mechanism unlike the one involving the 5' cap, at a sequence called the internal ribosome entry site. This process is not dependent on the full set of translation initiation factors (although this depends on the specific IRES) and is commonly found in the translation of viral mRNA. [9]
The ribosome can localize to the start site by direct binding, initiation factors, and/or ITAFs (IRES trans-acting factors) bypassing the need to scan the entire 5' UTR. This method of translation is important in conditions that require the translation of specific mRNAs during cellular stress, when overall translation is reduced.