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Li, V. DARS1 Gene. Encyclopedia. Available online: (accessed on 19 June 2024).
Li V. DARS1 Gene. Encyclopedia. Available at: Accessed June 19, 2024.
Li, Vivi. "DARS1 Gene" Encyclopedia, (accessed June 19, 2024).
Li, V. (2020, December 23). DARS1 Gene. In Encyclopedia.
Li, Vivi. "DARS1 Gene." Encyclopedia. Web. 23 December, 2020.
DARS1 Gene

Aspartyl-tRNA Synthetase: The DARS1 gene provides instructions for making an enzyme called aspartyl-tRNA synthetase. 


1. Normal Function

This enzyme is found in all cell types and plays an important role in the production (synthesis) of proteins. During protein synthesis, building blocks (amino acids) are connected together in a specific order, creating a chain of amino acids. A type of RNA called transfer RNA (tRNA) carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Aspartyl-tRNA synthetase attaches the amino acid aspartate to the correct tRNA, which helps ensure that aspartate is added at the proper place in proteins.

In addition to its role in protein synthesis, aspartyl-tRNA synthetase may have other functions that are not fully understood.

2. Health Conditions Related to Genetic Changes

2.1 Hypomyelination with Brainstem and Spinal Cord Involvement and Leg Spasticity

At least 16 mutations in the DARS1 gene have been found to cause a condition called hypomyelination with brainstem and spinal cord involvement and leg spasticity (HBSL). This condition is characterized by abnormalities of the nervous system's white matter, usually involving particular regions of the spinal cord and brainstem (the region of the brain that connects to the spinal cord). The white matter consists of nerve fibers covered by a fatty substance called myelin, which insulates the fibers and promotes the rapid transmission of nerve impulses. In HBSL, the nervous system has a reduced ability to form myelin (hypomyelination). Affected individuals develop muscle stiffness (spasticity) in the legs that worsens over time and impairs walking.

Most of the mutations in the DARS1 gene change single amino acids in the aspartyl-tRNA synthetase enzyme. These alterations occur in a region of the enzyme called the active site, where aspartate and the tRNA come together so the amino acid can be transferred. The altered enzyme has difficulty adding the amino acid to the tRNA, which in turn hinders the addition of aspartate to proteins. It is unclear how the gene mutations lead to the signs and symptoms of HBSL. Researchers do not understand why reduced activity of aspartyl-tRNA synthetase affects myelination or why specific parts of the brainstem and spinal cord are involved.

3. Other Names for This Gene

  • Asp tRNA Ligase

  • Aspartate tRNA Ligase

  • aspartate tRNA ligase 1, cytoplasmic

  • Aspartyl tRNA Synthetase

  • DARS

  • Synthetase, Aspartyl-tRNA


  1. Fröhlich D, Suchowerska AK, Voss C, He R, Wolvetang E, von Jonquieres G,Simons C, Fath T, Housley GD, Klugmann M. Expression Pattern of the Aspartyl-tRNASynthetase DARS in the Human Brain. Front Mol Neurosci. 2018 Mar 20;11:81. doi:10.3389/fnmol.2018.00081.
  2. Park SG, Choi EC, Kim S. Aminoacyl-tRNA synthetase-interacting multifunctionalproteins (AIMPs): a triad for cellular homeostasis. IUBMB Life. 2010Apr;62(4):296-302. doi: 10.1002/iub.324. Review.
  3. Taft RJ, Vanderver A, Leventer RJ, Damiani SA, Simons C, Grimmond SM, MillerD, Schmidt J, Lockhart PJ, Pope K, Ru K, Crawford J, Rosser T, de Coo IF, Juneja M, Verma IC, Prabhakar P, Blaser S, Raiman J, Pouwels PJ, Bevova MR, Abbink TE,van der Knaap MS, Wolf NI. Mutations in DARS cause hypomyelination with brainstem and spinal cord involvement and leg spasticity. Am J Hum Genet. 2013 May2;92(5):774-80. doi: 10.1016/j.ajhg.2013.04.006.
  4. Wolf NI, Toro C, Kister I, Latif KA, Leventer R, Pizzino A, Simons C, AbbinkTE, Taft RJ, van der Knaap MS, Vanderver A. DARS-associated leukoencephalopathycan mimic a steroid-responsive neuroinflammatory disorder. Neurology. 2015 Jan20;84(3):226-30. doi: 10.1212/WNL.0000000000001157.
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Update Date: 23 Dec 2020
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