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A ribosome is made from complexes of RNAs and proteins and is therefore a ribonucleoprotein complex. In prokaryotes each ribosome is composed of small (30S) and large (50S) components, called subunits, which are bound to each other: (30S) has mainly a decoding function and is also bound to the mRNA
50S, roughly equivalent to the 60S ribosomal subunit in eukaryotic cells, is the larger subunit of the 70S ribosome of prokaryotes. The 50S subunit is primarily composed of proteins but also contains single-stranded RNA known as ribosomal RNA (rRNA). rRNA forms secondary and tertiary structures to maintain the structure and carry out the catalytic functions of the ribosome.
The initiation phase is completed once a 50S subunit joins the 30S subunit, forming an active 70S ribosome. [11] Termination of the polypeptide occurs when the A site of the ribosome is occupied by a stop codon (UAA, UAG, or UGA) on the mRNA, creating the primary structure of a protein. tRNA usually cannot recognize or bind to stop codons.
A third protein, RaiA (ribosome-associated inhibitor A) is thought to both inactivate 70S ribosomes alone and stabilize them, preventing them from being converted into 100S ribosomes. [2] Most non-gammaproteobacteria, as well as some plant plastids, instead contain a HPF homologue that can form 100S ribosomes by itself. [2]
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:
[1] [2] Eukaryotic ribosomes are also known as 80S ribosomes, referring to their sedimentation coefficients in Svedberg units, because they sediment faster than the prokaryotic ribosomes. Eukaryotic ribosomes have two unequal subunits, designated small subunit (40S) and large subunit (60S) according to their sedimentation coefficients.
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 ...
Mitochondria and plastids contain their own ribosomes; these are more similar to those of bacteria (70S) than those of eukaryotes. [74] Proteins created by mitochondria and chloroplasts use N-formylmethionine as the initiating amino acid, as do proteins created by bacteria but not proteins created by eukaryotic nuclear genes or archaea. [75] [76]