Premium
Essentiality of threonylcarbamoyladenosine (t 6 A ), a universal t RNA modification, in bacteria
Author(s) -
Thiaville Patrick C.,
El Yacoubi Basma,
Köhrer Caroline,
Thiaville Jennifer J.,
Deutsch Chris,
IwataReuyl Dirk,
Bacusmo Jo Marie,
Armengaud Jean,
Bessho Yoshitaka,
Wetzel Collin,
Cao Xiaoyu,
Limbach Patrick A.,
RajBhandary Uttam L.,
CrécyLagard Valérie
Publication year - 2015
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13209
Subject(s) - biology , deinococcus radiodurans , thermus thermophilus , transfer rna , gene , genetics , escherichia coli , rna , deinococcus , bacteria
Summary Threonylcarbamoyladenosine (t 6 A ) is a modified nucleoside universally conserved in t RNA s in all three kingdoms of life. The recently discovered genes for t 6 A synthesis, including tsa C and tsa D , are essential in model prokaryotes but not essential in yeast. These genes had been identified as antibacterial targets even before their functions were known. However, the molecular basis for this prokaryotic‐specific essentiality has remained a mystery. Here, we show that t 6 A is a strong positive determinant for aminoacylation of t RNA by bacterial‐type but not by eukaryotic‐type isoleucyl‐t RNA synthetases and might also be a determinant for the essential enzyme t RNA Ile ‐lysidine synthetase. We confirm that t 6 A is essential in E scherichia coli and a survey of genome‐wide essentiality studies shows that genes for t 6 A synthesis are essential in most prokaryotes. This essentiality phenotype is not universal in Bacteria as t 6 A is dispensable in Deinococcus radiodurans , Thermus thermophilus , Synechocystis PCC 6803 and S treptococcus mutans . Proteomic analysis of t 6 A − D . radiodurans strains revealed an induction of the proteotoxic stress response and identified genes whose translation is most affected by the absence of t 6 A in t RNA s. Thus, although t 6 A is universally conserved in tRNAs, its role in translation might vary greatly between organisms.