Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major.

ABSTRACT:

Background

Leishmania major, a protozoan parasite, is the causative agent of cutaneous leishmaniasis. Due to the development of resistance against the currently available anti-leishmanial drugs, there is a growing need for specific inhibitors and novel drug targets. In this regards, aminoacyl tRNA synthetases, the linchpins of protein synthesis, have received recent attention among the kinetoplastid research community. This is the first comprehensive survey of the aminoacyl tRNA synthetases, their paralogs and other associated proteins from L. major.

Results

A total of 26 aminoacyl tRNA synthetases were identified using various computational and bioinformatics tools. Phylogenetic analysis and domain architectures of the L. major aminoacyl tRNA synthetases suggest a probable

SUBMITTER: Gowri VS 

PROVIDER: S-EPMC3532385 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature