Journal of Biological Chemistry
Volume 291, Issue 33, 12 August 2016, Pages 17102-17111
Journal home page for Journal of Biological Chemistry

Protein Synthesis and Degradation
Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation*

https://doi.org/10.1074/jbc.M116.734343Get rights and content
Under a Creative Commons license
open access

Arc1p is a yeast-specific tRNA-binding protein that forms a ternary complex with glutamyl-tRNA synthetase (GluRSc) and methionyl-tRNA synthetase (MetRS) in the cytoplasm to regulate their catalytic activities and subcellular distributions. Despite Arc1p not being involved in any known biotin-dependent reaction, it is a natural target of biotin modification. Results presented herein show that biotin modification had no obvious effect on the growth-supporting activity, subcellular distribution, tRNA binding, or interactions of Arc1p with GluRSc and MetRS. Nevertheless, biotinylation of Arc1p was temperature dependent; raising the growth temperature from 30 to 37 °C drastically reduced its biotinylation level. As a result, Arc1p purified from a yeast culture that had been grown overnight at 37 °C was essentially biotin free. Non-biotinylated Arc1p was more heat stable, more flexible in structure, and more effective than its biotinylated counterpart in promoting glutamylation activity of the otherwise inactive GluRSc at 37 °C in vitro. Our study suggests that the structure and function of Arc1p can be modulated via biotinylation in response to temperature changes.

aminoacyl tRNA synthetase
biotin
post-translational modification (PTM)
protein synthesis
transfer RNA (tRNA)

Cited by (0)

*

This work was supported by Grants MOST 103-2311-B-008-003-MY3, MOST 103-2923-B-008-001-MY3, and NSC 102-2311-B-008-004-MY3 (to C. C. W.) from the Ministry of Science and Technology (Taipei, Taiwan). The authors declare that they have no conflicts of interest with the contents of this article.