Messing up translation from the start: How AtaT inhibits translation initiation in E. coli

References

• Jurenas D, Chatterjee S, Konijnenberg A, Sobott F, Droogmans L, Garcia-Pino A, Van Melderen L. AtaT blocks translation initiation by N--acetylation of the initiator tRNAfMet. Nat Chem Biol. 2017;13:640–6. doi:10.1038/nchembio.2346.
   PubMed Web of Science ®Google Scholar
• Hayes F, Van Melderen L. Toxins--antitoxins: diversity, evolution and function. Crit Rev Biochem Mol Biol. 2011;46:386–408. doi:10.3109/10409238.2011.600437.
   PubMed Web of Science ®Google Scholar
• Page R, Peti W. Toxin--antitoxin systems in bacterial growth arrest and persistence. Nat Chem Biol. 2016;12:208–14. doi:10.1038/nchembio.2044.
   PubMed Web of Science ®Google Scholar
• Goeders N, Van Melderen L. Toxin--antitoxin systems as multilevel interaction systems. Toxins (Basel). 2014;6:304–24. doi:10.3390/toxins6010304.
   PubMed Web of Science ®Google Scholar
• Leplae R, Geeraerts D, Hallez R, Guglielmini J, Dreze P, Van Melderen L. Diversity of bacterial type II toxin--antitoxin systems: a comprehensive search and functional analysis of novel families. Nucleic Acids Res. 2011;39:5513–25. doi:10.1093/nar/gkr131.
   PubMed Web of Science ®Google Scholar
• Ramisetty BC, Santhosh RS. Horizontal gene transfer of chromosomal Type II toxin--antitoxin systems of Escherichia coli. FEMS Microbiol Lett. 2016;363.
   Web of Science ®Google Scholar
• Pandey DP, Gerdes K. Toxin--antitoxin loci are highly abundant in free--living but lost from host--associated prokaryotes. Nucleic Acids Res. 2005;33:966–76. doi:10.1093/nar/gki201.
   PubMed Web of Science ®Google Scholar
• Van Melderen L. Toxin--antitoxin systems: why so many, what for? Curr Opin Microbiol. 2010;13:781–5. doi:10.1016/j.mib.2010.10.006.
   PubMed Web of Science ®Google Scholar
• Van Melderen L, Saavedra De Bast M. Bacterial toxin--antitoxin systems: more than selfish entities? PLoS Genet. 2009;5:e1000437. doi:10.1371/journal.pgen.1000437.
   PubMed Web of Science ®Google Scholar
• Harms A, Maisonneuve E, Gerdes K. Mechanisms of bacterial persistence during stress and antibiotic exposure. Science. 2016;354. doi:10.1126/science.aaf4268.
   Web of Science ®Google Scholar
• Magnuson RD. Hypothetical functions of toxin--antitoxin systems. J Bacteriol. 2007;189:6089–92. doi:10.1128/JB.00958-07.
   PubMed Web of Science ®Google Scholar
• Yarmolinski MB. Programmed cell death in bacterial populations. Science. 1995;267:836–7. doi:10.1126/science.7846528.
   PubMed Web of Science ®Google Scholar
• Shan Y, Brown Gandt A, Rowe SE, Deisinger JP, Conlon BP, Lewis K. ATP-- Dependent Persister Formation in Escherichia coli. MBio. 2017;8. pii:e02267–16. doi:10.1128/mBio.02267-16.
   Web of Science ®Google Scholar
• Ramisetty BC, Ghosh D, Roy Chowdhury M, Santhosh RS. What Is the Link between Stringent Response, Endoribonuclease Encoding Type II Toxin--Antitoxin Systems and Persistence? Front Microbiol. 2016;7:1882. doi:10.3389/fmicb.2016.01882.
   PubMed Web of Science ®Google Scholar
• Van Melderen L, Wood TK. Commentary: What Is the Link between Stringent Response, Endoribonuclease Encoding Type II Toxin--Antitoxin Systems and Persistence? Front Microbiol. 2017;8:191. doi:10.3389/fmicb.2017.00191.
   PubMed Web of Science ®Google Scholar
• Bernard P, Couturier M. Cell killing by the F plasmid CcdB protein involves poisoning of DNA--topoisomerase II complexes. J Mol Biol. 1992;226:735–45. doi:10.1016/0022-2836(92)90629-X.
   PubMed Web of Science ®Google Scholar
• Zhang Y, Zhang J, Hoeflich KP, Ikura M, Qing G, Inouye M. MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol Cell. 2003;12:913–23. doi:10.1016/S1097-2765(03)00402-7.
   PubMed Web of Science ®Google Scholar
• Schifano JM, Edifor R, Sharp JD, Ouyang M, Konkimalla A, Husson RN, Woychik NA. Mycobacterial toxin MazF--mt6 inhibits translation through cleavage of 23S rRNA at the ribosomal A site. Proc Natl Acad Sci U S A. 2013;110:8501–6. doi:10.1073/pnas.1222031110.
   PubMed Web of Science ®Google Scholar
• Schifano JM, Cruz JW, Vvedenskaya IO, Edifor R, Ouyang M, Husson RN, Nickels BE, Woychik NA. tRNA is a new target for cleavage by a MazF toxin. Nucleic Acids Res. 2016;44:1256–70. doi:10.1093/nar/gkv1370.
   PubMed Web of Science ®Google Scholar
• Castro-Roa D, Garcia-Pino A, De Gieter S, van Nuland NAJ, Loris R, Zenkin N. The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF--Tu. Nat Chem Biol. 2013;9:811–7. doi:10.1038/nchembio.1364.
   PubMed Web of Science ®Google Scholar
• Harms A, Stanger FV, Scheu PD, de Jong IG, Goepfert A, Glatter T, Gerdes K, Schirmer T, Dehio C. Adenylylation of Gyrase and Topo IV by FicT Toxins Disrupts Bacterial DNA Topology. Cell Rep. 2015;12:1497–507. doi:10.1016/j.celrep.2015.07.056.
   PubMed Web of Science ®Google Scholar
• Lopes AP, Lopes LM, Fraga TR, Chura-Chambi RM, Sanson AL, Cheng E, Nakajima E, Morganti L, Martins EA. VapC from the leptospiral VapBC toxin--antitoxin module displays ribonuclease activity on the initiator tRNA. PLoS One. 2014;9:e101678. doi:10.1371/journal.pone.0101678.
   PubMed Web of Science ®Google Scholar
• Winther K, Tree JJ, Tollervey D, Gerdes K. VapCs of Mycobacterium tuberculosis cleave RNAs essential for translation. Nucleic Acids Res. 2016;44:9860–71. doi:10.1093/nar/gkw781.
   PubMed Web of Science ®Google Scholar
• Winther KS, Brodersen DE, Brown AK, Gerdes K. VapC20 of Mycobacterium tuberculosis cleaves the sarcin--ricin loop of 23S rRNA. Nat Commun. 2013;4:2796. doi:10.1038/ncomms3796.
   PubMed Web of Science ®Google Scholar
• Winther KS, Gerdes K. Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA. Proc Natl Acad Sci U S A. 2011;108:7403–7. doi:10.1073/pnas.1019587108.
   PubMed Web of Science ®Google Scholar
• Laursen BS, Sorensen HP, Mortensen KK, Sperling-Petersen HU. Initiation of protein synthesis in bacteria. Microbiol Mol Biol Rev. 2005;69:101–23. doi:10.1128/MMBR.69.1.101-123.2005.
   PubMed Web of Science ®Google Scholar
• Seong BL, RajBhandary UL. Mutants of Escherichia coli formylmethionine tRNA: a single base change enables initiator tRNA to act as an elongator in vitro. Proc Natl Acad Sci U S A. 1987;84:8859–63. doi:10.1073/pnas.84.24.8859.
   PubMed Web of Science ®Google Scholar
• Varshney U, Lee CP, RajBhandary UL. From elongator tRNA to initiator tRNA. Proc Natl Acad Sci U S A. 1993;90:2305–9. doi:10.1073/pnas.90.6.2305.
   PubMed Web of Science ®Google Scholar
• Seong BL, RajBhandary UL. Escherichia coli formylmethionine tRNA: mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop. Proc Natl Acad Sci U S A. 1987; 84:334–8. doi:10.1073/pnas.84.2.334.
   PubMed Web of Science ®Google Scholar
• Iqbal N, Guerout AM, Krin E, Le Roux F, Mazel D. Comprehensive Functional Analysis of the 18 Vibrio cholerae N16961 Toxin--Antitoxin Systems Substantiates Their Role in Stabilizing the Superintegron. J Bacteriol. 2015;197:2150–9. doi:10.1128/JB.00108-15.
   PubMed Web of Science ®Google Scholar
• Cheverton AM, Gollan B, Przydacz M, Wong CT, Mylona A, Hare SA, Helaine S. A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA. Mol Cell. 2016;63:86–96. doi:10.1016/j.molcel.2016.05.002.
   PubMed Web of Science ®Google Scholar
• McVicker G, Tang CM. Deletion of toxin--antitoxin systems in the evolution of Shigella sonnei as a host--adapted pathogen. Nat Microbiol. 2016;2:16204. doi:10.1038/nmicrobiol.2016.204.
   PubMed Web of Science ®Google Scholar
• Van Acker H, Sass A, Dhondt I, Nelis HJ, Coenye T. Involvement of toxin--antitoxin modules in Burkholderia cenocepacia biofilm persistence. Pathog Dis. 2014;71:326–35. doi:10.1111/2049-632X.12177.
   PubMed Web of Science ®Google Scholar
• Jurenas D, Garcia-Pino A, Van Melderen L. Novel toxins from type II toxin-- antitoxin systems with acetyltransferase activity. Plasmid. 2017;93:30–5. doi:10.1016/j.plasmid.2017.08.005.
   PubMed Web of Science ®Google Scholar
• Helaine S, Cheverton AM, Watson KG, Faure LM, Matthews SA, Holden DW. Internalization of Salmonella by macrophages induces formation of nonreplicating persisters. Science. 2014;343:204–8. doi:10.1126/science.1244705.
   PubMed Web of Science ®Google Scholar
• Janiak F, Dell VA, Abrahamson JK, Watson BS, Miller DL, Johnson AE. Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis. Biochemistry. 1990;29:4268–77. doi:10.1021/bi00470a002.
   PubMed Web of Science ®Google Scholar
• Favrot L, Blanchard JS, Vergnolle O. Bacterial GCN5--Related N--Acetyltransferases: From Resistance to Regulation. Biochemistry. 2016;55:989–1002. doi:10.1021/acs.biochem.5b01269.
   PubMed Web of Science ®Google Scholar
• Salah Ud-Din AI, Tikhomirova A, Roujeinikova A. Structure and Functional Diversity of GCN5--Related N--Acetyltransferases (GNAT). Int J Mol Sci. 2016;17. doi:10.3390/ijms17071018.
   PubMed Web of Science ®Google Scholar
• Sharma S, Kaushik S, Sinha M, Kushwaha GS, Singh A, Sikarwar J, Chaudhary A, Gupta A, Kaur P, Singh TP. Structural and functional insights into peptidyl--tRNA hydrolase. Biochim Biophys Acta. 2014;1844:1279–88. doi:10.1016/j.bbapap.2014.04.012.
   PubMed Web of Science ®Google Scholar
• Pedersen K, Zavialov AV, Pavlov MY, Elf J, Gerdes K, Ehrenberg M. The bacterial toxin RelE displays codon--specific cleavage of mRNAs in the ribosomal A site. Cell. 2003;112:131–40. doi:10.1016/S0092-8674(02)01248-5.
   PubMed Web of Science ®Google Scholar
• Ainelo A, Tamman H, Leppik M, Remme J, Horak R. The toxin GraT inhibits ribosome biogenesis. Mol Microbiol. 2016;100:719–34. doi:10.1111/mmi.13344.
   PubMed Web of Science ®Google Scholar
• Germain E, Castro-Roa D, Zenkin N, Gerdes K. Molecular mechanism of bacterial persistence by HipA. Mol Cell. 2013;52:248–54. doi:10.1016/j.molcel.2013.08.045.
   PubMed Web of Science ®Google Scholar
• Kaspy I, Rotem E, Weiss N, Ronin I, Balaban NQ, Glaser G. HipA-mediated antibiotic persistence via phosphorylation of the glutamyl--tRNA--synthetase. Nat Commun. 2013;4:3001. doi:10.1038/ncomms4001.
   PubMed Web of Science ®Google Scholar