Abstract
During protein synthesis, there are several checkpoints in the cell to ensure that the information encoded within genetic material is decoded correctly. Charging of tRNA with its cognate amino acid is one of the important steps in protein synthesis and is carried out by aminoacyl-tRNA synthetase (aaRS) with great accuracy. However, due to presence of D-amino acids in the cell, sometimes aaRS charges tRNA with D-amino acids resulting in the hampering of protein translational process, which is lethal to the cell. Every species has some mechanism in order to prevent the formation of D-amino acid-tRNA complex, for instance DTD (D-Tyr-tRNA deacylase) is an enzyme responsible for the cleavage of ester bond formed between D-amino acid and tRNA leading to error free translation process. In this review, structure, function, and enzymatic mechanism of DTD are discussed. The role of DTD as a drug target is also considered.
Highlights
Protein synthesis process results in the production of functional proteins and the accuracy of this process determines the fate of the cell
In some cases, aminoacyl-tRNA synthetase (aaRS) may tag tRNA with D-amino acids (Giegé et al, 1998; Yadavalli and Ibba, 2012) resulting into the formation of D-aa-tRNA complex
The complex is very lethal and in order to rescue cell, formed D-aa-tRNA complex must be cleaved to release tRNA molecules (Soutourina et al, 1999, 2004) and it is done by the proofreading activity of D-Tyr-tRNA deacylase (DTD) responsible for hydrolyzing D-aa-tRNA complex
Summary
Protein synthesis process results in the production of functional proteins and the accuracy of this process determines the fate of the cell. The complex is very lethal and in order to rescue cell, formed D-aa-tRNA complex must be cleaved to release tRNA molecules (Soutourina et al, 1999, 2004) and it is done by the proofreading activity of D-Tyr-tRNA deacylase (DTD) responsible for hydrolyzing D-aa-tRNA complex. It causes the cleavage of bond formed between D-amino acids and tRNA making tRNA available to coalesce with L-amino acids (Wydau et al, 2009; Zheng et al, 2009). The possibility of DTD as a drug target will be accentuated
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