Translation is the process in living cells in which proteins are produced using RNA molecules as templates. The generated protein is a sequence of amino acids. This sequence is determined by the sequence of nucleotides in the RNA. The nucleotides are considered three at a time. Each such triple results in addition of one specific amino acid to the protein being generated. The matching from nucleotide triple to amino acid is called the genetic code. The translation is performed by a large complex of functional RNA and proteins called ribosomes. The entire process is called gene expression.
Prokaryotes The three steps of prokaryotic translation are initiation, elongation, and termination. It’s the procedure of the synthesis of proteins based on mRNA information. The enzymes aminoacyl transfer RNA synthesis is involved in protein synthesis. The translation is a process of concurrently generating proteins and transcription in prokaryotes. After the 5′ end of both the gene is transcribed into mRNA, translation begins.
Translation in prokaryotes is divided into three stages: initiation, elongation, and termination. The two subunits, the 50S & 30S, are united to start the translation process. IF1, IF2, and IF3 are three initiating factors that aid in forming the forms of a complex. The first amino acid added during translation is N-formylmethionine.
The power source for the synthesis of peptide bonds between the surviving plus arriving nucleotides is GTP. EF-P is the translation initiation factor. The ribosome’s interaction with the Shine-Dalgarno sequence facilitates the identification of the start codon. A purine-rich region positioned ahead of the AUG initiation codon is Known as the Shine-Dalgarno motif. The pyrimidine-rich region of 16S rRNA is complementary to this sequence. The 30S subunit contains the 16S rRNA.
The double RNA structure is formed when these two complementary nucleotides bind together. The initiation codon is brought into the ribosome’s P-site by this pairing. The first amino acid binds the P site. There are three active sites on a ribosome: A, P, and E. Other than the last aminoacyl tRNA, all incoming aminoacyl tRNAs bind to the A site. The P site is where the peptide bond is formed. The E site is the uncharged tRNA’s exit point.
Eukaryotes The systematic framework of events that involves the tRNA is known as eukaryotic translation. In a eukaryotic creature, it is transcribed into protein. In eukaryotes, this translation is a four-step procedure with four steps. Gene regulation, elongation, termination, and recycling are the four steps. It’s a cyclic process in which post-termination ribosomal complexes are cyclically recycled to produce ribosomal subunits.
The second phase of eukaryotes gene regulation, translation, is distinct from eukaryotic transcription. In eukaryotic, transcription and translation take place in two separate compartments. As a result, the two methods never occur simultaneously. Eukaryotic mRNAs do seem to be monocistronic and therefore are processed in the nucleus before being released to the cytoplasm by appending a 5′ cap, poly A tail, and splicing out introns. By co-translational folding of the freshly formed polypeptide on the ribosome, ribosomal stalling impacts translation. This method pauses translation, allowing for more time to be spent on it. A 5′ cap and a poly-A tail are found on eukaryotic mRNAs.
As a result, there are two types of translation initiation: cap-dependent beginning and cap-independent introduction. The initiation has somewhere to the 5′ end during cap-dependent initiation. These initiating factors keep the mRNA in the ribosome’s small subunit. Internal ribosome entering sites allow direct ribosome transportation to the origin of replication during cap-independent initiation. Methionine is the first interacting amino acid in eukaryotes. The 40S and 60S subunits combine to generate the 80S ribosome.