The pseudo-dimeric tyrosyl-tRNA synthetase of T. brucei aminoacylates cytosolic and mitochondrial tRNA Tyr and requires both monomeric units for activity

Käser, Sandro; Glauser, Isabelle; Rettig, Jochen; Schneider, André (2018). The pseudo-dimeric tyrosyl-tRNA synthetase of T. brucei aminoacylates cytosolic and mitochondrial tRNA Tyr and requires both monomeric units for activity. Molecular and biochemical parasitology, 221, pp. 52-55. Elsevier 10.1016/j.molbiopara.2018.03.004

[img] Text
1-s2.0-S0166685118300215-main.pdf - Published Version
Restricted to registered users only
Available under License Publisher holds Copyright.

Download (874kB) | Request a copy
[img]
Preview
Text
TyrRS-revised.pdf - Accepted Version
Available under License Creative Commons: Attribution-Noncommercial-No Derivative Works (CC-BY-NC-ND).

Download (2MB) | Preview

Aminoacyl-tRNA synthetases are essential for protein synthesis. The single-copy tyrosyl-tRNA synthetase (Tb-TyrRS) of T. brucei has an unusual structure and forms a pseudo-dimer. It is therefore twice the size than tyrosyl-tRNA synthetases of most other organisms. Here we show by inducible RNAi that Tb-TyrRS is essential for normal growth of procyclic T. brucei. Furthermore we demonstrate that Tb-TyrRS aminoacylates cytosolic as well as mitochondrial tRNATyr indicating that it is dually localized. Finally we show that individual deletion of the 36 N- or C-terminal amino acids abolishes the function of Tb-TyrRS. This indicates that both monomeric units of the enzyme, the C-terminal one of which is predicted to lack enzymatic activity, are essential for Tb-TyrRS function. In summary our results together with previous studies support the notion that Tb-TyrRS might be a suitable drug target.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)

UniBE Contributor:

Käser, Sandro, Glauser, Isabelle, Rettig, Jochen Peter, Schneider, André

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

0166-6851

Publisher:

Elsevier

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

02 May 2018 10:59

Last Modified:

02 Mar 2023 23:30

Publisher DOI:

10.1016/j.molbiopara.2018.03.004

BORIS DOI:

10.7892/boris.113606

URI:

https://boris.unibe.ch/id/eprint/113606

Actions (login required)

Edit item Edit item
Provide Feedback