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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 30S subunit is an integral part of mRNA translation.It binds three prokaryotic initiation factors: IF-1, IF-2, and IF-3. [3]A portion of the 30S subunit (the 16S rRNA) guides the initiating start codon (5′)-AUG-(3′) of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. [4]
This accounts for why fragment names do not add up: for example, bacterial 70S ribosomes are made of 50S and 30S subunits. Prokaryotes have 70S ribosomes, each consisting of a small and a large subunit. E. coli, for example, has a 16S RNA subunit (consisting of 1540 nucleotides) that is bound to 21 proteins.
In the small (30S) subunit of E. coli ribosomes, the proteins denoted uS4, uS7, uS8, uS15, uS17, bS20 bind independently to 16S rRNA. After assembly of these primary binding proteins, uS5, bS6, uS9, uS12, uS13, bS16, bS18, and uS19 bind to the growing ribosome. These proteins also potentiate the addition of uS2, uS3, uS10, uS11, uS14, and bS21.
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.
Ribosome recycling step is responsible for the disassembly of the post-termination ribosomal complex. [14] Once the nascent protein is released in termination, Ribosome Recycling Factor and Elongation Factor G (EF-G) function to release mRNA and tRNAs from ribosomes and dissociate the 70S ribosome into the 30S and 50S subunits. IF3 then ...
[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.
Quinupristin binds to a nearby site on the 50S ribosomal subunit and prevents elongation of the polypeptide, [9] as well as causing incomplete chains to be released. [9] Geneticin, also called G418, inhibits the elongation step in both prokaryotic and eukaryotic ribosomes. [10]