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During translation elongation, tRNA first binds to the ribosome as part of a complex with elongation factor Tu or its eukaryotic or archaeal counterpart. This initial tRNA binding site is called the A/T site. In the A/T site, the A-site half resides in the small ribosomal subunit where the mRNA decoding site is located.
For example, if the amino acid that attach to the end is phenylalanine, the reaction will be catalyzed by phenylalanine-tRNA synthase to produce tRNA phe. [4] The other end—the bottom often called the "DNA arm"—consists of a three base sequence that pairs with a complementary base sequence in a mRNA. [5]
All together, the actual stability of the ester bond influences the susceptibility of the aa-tRNA to hydrolysis within the body at physiological pH and ion concentrations. It is thermodynamically favorable that the aminoacylation process yield a stable aa-tRNA molecule, thus providing for the acceleration and productivity of polypeptide synthesis.
The amino acid is joined by its carboxyl group to the 3' OH of the tRNA by an ester bond. When the tRNA has an amino acid linked to it, the tRNA is termed "charged". In bacteria, this aminoacyl-tRNA is carried to the ribosome by EF-Tu, where mRNA codons are matched through complementary base pairing to specific tRNA anticodons. Aminoacyl-tRNA ...
The T-arm or T-loop is a specialized region on the tRNA molecule which acts as a special recognition site for the ribosome to form a tRNA-ribosome complex during protein biosynthesis or translation (biology). The T-arm has two components to it; the T-stem and the T-loop.
Unlike double-stranded DNA, RNA is usually a single-stranded molecule (ssRNA) [4] in many of its biological roles and consists of much shorter chains of nucleotides. [5] However, double-stranded RNA (dsRNA) can form and (moreover) a single RNA molecule can, by complementary base pairing, form intrastrand double helixes, as in tRNA.
In the mid-1960s, the role of tRNA in protein synthesis was being intensively studied. In 1965, Holley et al. purified and sequenced the first tRNA molecule, initially proposing that it adopted a cloverleaf structure, based largely on the ability of certain regions of the molecule to form stem loop structures. [60]
Mitochondrially encoded tRNA glutamic acid also known as MT-TE is a transfer RNA which in humans is encoded by the mitochondrial MT-TE gene. [1] MT-TE is a small 69 nucleotide RNA (human mitochondrial map position 14674–14742) that transfers the amino acid glutamic acid to a growing polypeptide chain at the ribosome site of protein synthesis during translation.