Aminoacyl tRNA synthetase

Aminoacyl tRNA synthetase (AARS) is a group of enzymes that play a crucial role in protein synthesis. These enzymes are responsible for attaching each amino acid to its corresponding transfer RNA (tRNA) molecule. This process is a key step in the translation of messenger RNA (mRNA) into protein.

Function

Aminoacyl tRNA synthetases catalyze the esterification of a specific amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. This is sometimes referred to as "charging" the tRNA with the amino acid. Once the tRNA is charged, it can transfer the amino acid to the growing polypeptide chain during protein synthesis.

Classification

Aminoacyl tRNA synthetases can be classified into two classes, I and II, based on their structural properties. Class I AARSs contain a Rossmann fold catalytic domain and attach the amino acid to the 2'-OH of the tRNA, while Class II AARSs have an antiparallel beta-sheet domain and attach the amino acid to the 3'-OH. Each class is further divided into three subclasses.

Role in Disease

Mutations in genes encoding aminoacyl tRNA synthetases have been associated with a variety of human diseases, including Charcot-Marie-Tooth disease, distal spinal muscular atrophy, and hypomyelinating leukodystrophy. Understanding the role of these enzymes in disease can provide insights into the molecular mechanisms of these disorders and potential therapeutic strategies.

See Also

• Protein biosynthesis
• Transfer RNA
• Translation (biology)

References

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