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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 50S (large prokaryotic) subunit was determined from the archaeon Haloarcula marismortui [39] and the bacterium Deinococcus radiodurans, and the structure of the 30S subunit was determined from the bacterium Thermus thermophilus. [16] [40] These structural studies were awarded the Nobel Prize in Chemistry in 2009.
This ribosomal protein is a component of the 50S subunit. The protein binds 5S rRNA to form a stable complex. In turn 5S rRNA binds specifically to three proteins, L25, L18 and L5, forming a separate domain of the bacterial ribosome. [1] Protein L25 of E. coli is not essential for survival of the cells. [2] [3]
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 from all organisms share a highly conserved catalytic center. However, the ribosomes of eukaryotes (animals, plants, fungi, and large number unicellular organisms all with a nucleus) are much larger than prokaryotic (bacterial and archaeal) ribosomes and subject to more complex regulation and biogenesis pathways.
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]
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:
This is a view of the 3D arrangement of the 23S and 5S rRNA in the Escherichia coli 50S ribosomal subunit based on a cryo-electron microscopic reconstruction. [1] The 23S rRNA is a 2,904 nucleotide long (in E. coli) component of the large subunit of the bacterial/archean ribosome and makes up the peptidyl transferase center (PTC). [2]