HARS2: A Mitochondrial Protein Involved in TRNA Ligase and Protein Synthesis

Target Name: HARS2

NCBI ID: G23438

HARS2

HARS2: A Mitochondrial Protein Involved in TRNA Ligase and Protein Synthesis

Histidine tRNA Ligase 2 (HARS2), a protein encoded in the mitochondrial genome, is a key enzyme in the regulation of mitochondrial protein synthesis. HARS2 plays a crucial role in the transfer of histidine residues from the amino acid lysine to the tRNA during the process of translation. As a result, HARS2 is highly conserved across various species, including bacteria, archaea, and eukaryotes.

HARS2 functions as a mitochondrial protein that localizes to the cytoplasm, where it is involved in the delivery of amino acids to the cytoplasmic side of the mitochondrial matrix during the process of translation. It does this by using a unique protein-protein interaction, where it interacts with the cytoplasmic domain of the protein SIR2.

SIR2 is a cytoplasmic protein that belongs to the family of NAD+-dependent enzymes, known as NAD+-dependent enzymes. These enzymes use nicotinamide adenine dinucleotide (NAD+) as a cofactor to convert NAD+ to NADH, which is then used as a source of energy for the cell's metabolic processes.

HARS2 and SIR2 have been shown to interact in a highly conserved manner, as they share a common catalytic core and a conserved active site. This interaction allows for the transfer of histidine residues from the amino acid lysine to the tRNA during the process of translation.

One of the unique features of HARS2 is its ability to transfer multiple histidine residues to tRNA in a single transaction. This is critical for the efficient delivery of histidine residues to the cytoplasmic side of the mitochondrial matrix during translation.

In addition to its role in the delivery of histidine residues, HARS2 is also involved in the regulation of mitochondrial protein synthesis. This is accomplished through its interaction with the rRNA domain of the protein Mg2+-ATPase. HARS2 and Mg2+-ATPase form a protein-protein interaction, which allows for the regulation of Mg2+-ATPase activity and the subsequent control of mitochondrial protein synthesis.

HARS2 is also involved in the regulation of mitochondrial translation efficiency. This is accomplished through its interaction with the eIF4F complex, which is responsible for the initiation of the translation process. HARS2 and eIF4F form a protein-protein interaction, which allows for the regulation of eIF4F activity and the subsequent control of mitochondrial translation efficiency.

HARS2 is a highly conserved protein that is involved in the regulation of various cellular processes in the cell. Its role in the delivery of histidine residues to the cytoplasmic side of the mitochondrial matrix during translation and its involvement in the regulation of mitochondrial protein synthesis and translation efficiency make it an attractive drug target or biomarker.

In conclusion, HARS2 is a highly conserved protein that plays a critical role in the regulation of mitochondrial protein synthesis. Its ability to transfer multiple histidine residues to tRNA during the process of translation and its involvement in the regulation of mitochondrial translation efficiency make it an attractive drug target or biomarker. Further research is needed to fully understand the mechanisms of HARS2's function in the cell and its potential as a drug target.

Protein Name: Histidyl-tRNA Synthetase 2, Mitochondrial

Functions: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP)

The "HARS2 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about HARS2 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets