TyrRS

Tyrosyl-tRNA synthetase, often abbreviated as TyrRS, is an enzyme that plays a crucial role in protein synthesis. It belongs to the family of aminoacyl-tRNA synthetases, which are responsible for attaching the correct amino acid to its corresponding transfer RNA (tRNA) molecule. Specifically, TyrRS catalyzes the attachment of the amino acid tyrosine to its cognate tRNA, which is denoted as tRNA(Tyr). This process, known as aminoacylation or charging, is a vital step in the translation of genetic information from messenger RNA (mRNA) into proteins.

The reaction catalyzed by TyrRS involves two main steps. First, the enzyme activates tyrosine by forming tyrosyl adenylate, using ATP as an energy source. Second, the activated tyrosine is transferred to the 3' acceptor stem of tRNA(Tyr). This precise recognition and attachment ensure the fidelity of protein synthesis, as an incorrect amino acid attached to a tRNA would lead to a non-functional or faulty protein.

Beyond its canonical role in translation, TyrRS has also been found to possess non-canonical functions. These extraribosomal activities are not directly involved in protein synthesis but contribute to various cellular processes. For instance, TyrRS can interact with other proteins and nucleic acids, participating in signaling pathways, immune responses, and even acting as a cytokine. These dual roles highlight the complexity and versatility of TyrRS within the cell. Mutations in the gene encoding TyrRS can lead to a range of genetic disorders, underscoring its importance for human health.