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Updated: Aug 18, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Class-specific binding of two aminoacyl-tRNA synthetases to annexin, a Ca2+- and phospholipid-binding protein
Tomohiro Shirakawa1, Akio Nakamura, Kazuhiro Kohama
1Graduate School of Science, Biological Science, Osaka University, Japan.
Abstract:
Annexins are a family of Ca2+/phospholipid-binding proteins that have diverse functions. To understand the function of annexin in Physarum polycephalum, we searched for its binding proteins. Here we demonstrate the presence of two novel annexin-binding proteins. The homology search of partial amino acid sequences of these two proteins identified them as aminoacyl-tRNA synthetases (ARSs). Furthermore, antibody against aminoacyl-tRNA synthetases cross-reacted with one of two proteins. Our results imply the interaction between intracellular membrane dynamics and protein translation system, and may give a clue to understand the mechanism of some myositis diseases, which have been known to produce autoantibodies against ARSs.
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