Premium
Regulation of translational fidelity and neurodegeneration
Author(s) -
Ackerman Susan L.
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.526.1
Subject(s) - neurodegeneration , gene , aminoacyl trna synthetase , transfer rna , mutation , biology , protein biosynthesis , computational biology , genetics , rna , medicine , disease , pathology
The faithful execution of protein production from mRNAs is largely controlled by accurate charging of tRNAs by the aminoacyl tRNA tRNA synthetases. Many of these enzymes have editing domains that can recognize and correct mischarging of cognate tRNAs. We previously identified a spontaneous mutation in the editing domain of the mouse alanyl tRNA‐synthetase gene which leads to aggregates of misfolded proteins and degeneration of cerebellar Purkinje cells. By forward genetics we have identified a modifier gene of this mutation that prevents aggregate formation and neurodegeneration. Our data demonstrates that this novel vertebrate‐specific protein plays an important, previously unappreciated role in translational fidelity. Support or Funding Information This work was supported by NIH and Howard Hughes Medical Institute.