DARS

Official Full Name

aspartyl-tRNA synthetase 1

Organism

Homo sapiens

Gene ID

1615

Background

This gene encodes a member of a multienzyme complex that functions in mediating the attachment of amino acids to their cognate tRNAs. The encoded protein ligates L-aspartate to tRNA(Asp). Mutations in this gene have been found in patients showing hypomyelination with brainstem and spinal cord involvement and leg spasticity. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2014]

Synonyms

DARS1; DARS; HBSL; aspRS

Cat.No.	Product Name	Price
CSC-DC004030	Panoply™ Human DARS Knockdown Stable Cell Line	Inquiry
CSC-SC004030	Panoply™ Human DARS Over-expressing Stable Cell Line	Inquiry

Cat.No.	Product Name	Price
AD04588Z	Human DARS adenoviral particles	Inquiry
LV10299L	human DARS (NM_001349) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHH274601	shRNA set against Human DARS (NM_001349.2)	Inquiry
SHH274605	shRNA set against Mouse DARS (NM_177445.5)	Inquiry
SHH274609	shRNA set against Rat DARS (NM_053799.2)	Inquiry
SHW000608	shRNA set against Chicken DARS (NM_001006528)	Inquiry
SHW010691	shRNA set against Danio rerio DARS (NM_001077611)	Inquiry

Cat.No.	Product Name	Price
CDCB162083	Chicken DARS ORF Clone (NM_001006528)	Inquiry
CDFH004760	Human DARS cDNA Clone(NM_001349.2)	Inquiry
CDFL003433	Mouse Dars cDNA Clone(NM_145507.2)	Inquiry
CDFR013541	Rat Dars cDNA Clone(NM_053799.2)	Inquiry
MiUTR1H-02670	DARS miRNA 3'UTR clone	Inquiry
CDCB159225	Human DARS ORF clone (BC000629)	Inquiry
CDCB172166	Danio rerio DARS ORF Clone (NM_001077611)	Inquiry
CDCB191096	Rabbit DARS ORF clone (XM_002712122.2)	Inquiry
CDCR053494	Mouse Dars ORF clone (NM_145507.2)	Inquiry
CDCR273944	Mouse Dars ORF Clone(NM_177445.5)	Inquiry
CDCR280588	Human DARS ORF Clone(NM_001349.2)	Inquiry
CDCR380573	Rat Dars ORF Clone(NM_053799.2)	Inquiry
CDCS410242	Human DARS ORF Clone (BC000629)	Inquiry

Detailed Information

Aspartyl-tRNA synthetase (Dars) is a vital enzyme involved in protein synthesis, specifically in the process of tRNA aminoacylation. This enzyme belongs to the aminoacyl-tRNA synthetase family, responsible for catalyzing the attachment of specific amino acids to their corresponding tRNA molecules, a fundamental step in translation. Dars specifically charges tRNA molecules with aspartic acid, ensuring their accurate incorporation into nascent polypeptide chains during protein synthesis. By recognizing the unique structure of aspartic acid and the corresponding tRNA, Dars plays a critical role in maintaining the fidelity and efficiency of the translation process. Moreover, emerging research indicates that Dars might possess additional functions beyond its canonical role in translation, implicating it in various cellular processes and diseases.

Dars: Facilitating Precision in Protein Synthesis

Aspartyl-tRNA synthetase (Dars) is a key enzyme in the process of translation, ensuring the accurate incorporation of aspartic acid into growing polypeptide chains. As a member of the aminoacyl-tRNA synthetase family, Dars specifically charges its cognate tRNA molecules with aspartic acid, a crucial step for the fidelity of translation. During protein synthesis, Dars recognizes the unique structural features of aspartic acid and the corresponding tRNA, catalyzing their precise pairing. By meticulously facilitating this aminoacylation process, Dars plays a fundamental role in maintaining the integrity and functionality of cellular proteins. Its accuracy in ensuring the correct amino acid incorporation underscores its significance in the synthesis of functional proteins essential for various biological processes.

Dars: Beyond Translation, Unraveling Its Role in Cell Signaling

Aspartyl-tRNA synthetase (Dars), traditionally recognized for its involvement in protein synthesis, has recently emerged as a multifunctional enzyme with roles extending beyond translation. Studies indicate that Dars participates in cell signaling processes, potentially influencing various cellular pathways. One of its newfound functions involves modulating the mTOR (mechanistic Target of Rapamycin) signaling pathway, a crucial regulator of cell growth and metabolism. Dars interacts with components of the mTOR complex, suggesting its involvement in the intricate network of cellular signaling cascades. Moreover, recent research has linked Dars to stress response pathways, indicating its potential role in cellular adaptation to environmental challenges.

Dars and Cancer: Unraveling the Link

Aspartyl-tRNA synthetase (Dars) has gained attention in cancer research due to its emerging association with tumorigenesis and cancer progression. Studies have revealed altered expression levels and dysregulated activities of Dars in various cancer types. Dysfunctional Dars has been implicated in promoting cancer cell survival, proliferation, and invasion. It is also involved in regulating the translation of specific mRNA transcripts critical for cancer cell growth. Moreover, Dars interacts with components of cellular signaling pathways that play pivotal roles in cancer development.

Additionally, recent research has highlighted the potential of Dars as a therapeutic target. Modulating Dars activity or targeting its interactions in cancer cells holds promise for developing innovative anticancer strategies. Understanding the intricate relationship between Dars and cancer provides valuable insights into the molecular mechanisms underlying tumorigenesis, offering avenues for targeted therapies and personalized treatment approaches in the fight against cancer.

References:

Gu, Xuan et al. "Aspartyl-tRNA synthetase 2 orchestrates iron-sulfur metabolism in hematopoietic stem cells via fine-tuning alternative RNA splicing." Cell reports, vol. 42,10 113264. 13 Oct. 2023, doi:10.1016/j.celrep.2023.113264
Feng, Cong-Hua et al. "Aspartyl tRNA-synthetase (Dars) gene family enhances drought tolerance in poplar through BABA-PtrIBIs-PtrVOZ signaling module." BMC genomics vol. 24,1 473. 21 Aug. 2023, doi:10.1186/s12864-023-09556-2

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