Large-Scale Movement of Functional Domains Facilitates Aminoacylation by Human Mitochondrial Phenylalanyl-tRNA Synthetase

Authors

Srujana S. Yadavalli, The Ohio State University
Liron Klipcan, Weizmann Institute of Science
Alexey Zozulya, EMBL, Hamburg Outstation
Ranat Banerjee, The Ohio State University
Dmitri Svergun, EMBL, Hamburg Outstation
Mark Safro, Weizmann Institute of Science
Michael Ibba, Chapman UniversityFollow

Document Type

Article

Publication Date

9-6-2009

Abstract

Structural studies suggest rearrangement of the RNA‐binding and catalytic domains of human mitochondrial PheRS (mtPheRS) is required for aminoacylation. Crosslinking the catalytic and RNA‐binding domains resulted in a “closed” form of mtPheRS that still catalyzed ATP‐dependent Phe activation, but was no longer able to transfer Phe to tRNA and complete the aminoacylation reaction. SAXS experiments indicated the presence of both the closed and open forms of mtPheRS in solution. Together, these results indicate that conformational flexibility of the two functional modules in mtPheRS is essential for its phenylalanylation activity. This is consistent with the evolution of the aminoacyl‐tRNA synthetases as modular enzymes consisting of separate domains that display independent activities.

Comments

This article was originally published in FEBS Letters, volume 583, in 2009. https://doi.org/10.1016/j.febslet.2009.09.008

Recommended Citation

Yadavalli, S.S., Klipcan, L., Zozulya, A., Banerjee, R., Svergun, D. Safro, M. Ibba, M. (2009) Large-scale movement of functional domains facilitates aminoacylation by human mitochondrial phenylalanyl-tRNA synthetase. FEBS Lett. 583, 3204-3208. https://doi.org/10.1016/j.febslet.2009.09.008

Copyright

Federation of European Biochemical Societies