DaRS Background Information Aminoacyl-tRNA synthetases consist of a family of enzymes that catalyze the specific aminoacylation of cognate tRNA in the initial step of ribosome-dependent protein biosynthesis. DaRS is part of a multisubunit complex of aminoacyl-tRNA synthetases and is involved in the transfer of Asp-tRNA to EF-1 å1 (elongation factor alpha 1). The N-terminus of DaRS in vertebrates is a newly evolved structure that contains a putative amphiphilic helix and is dissimilar between different species. The N-terminal extension acts as a switch that, when in its stretched form, reduces the rate of dissociation of Asp-tRNA from DaRS, thereby providing enough time for EF-1 å1 to interact with Asp-tRNA. This suggests that the N-terminus of DaRS plays a critical role in its catalytic function. DaRS contains two phosphorylations sites, forms homodimers and localizes to the cytoplasm.
DaRS (14S6)
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DaRS (14S6): sc-100986. Immunoperoxidase staining of formalin-fixed, paraffin-embedded human colon tissue showing cytoplasmic localization.
DaRS (14S6): sc-100986. Western blot analysis of DaRS expression in HeLa whole cell lysate.
