tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial Pathogens
Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modi...
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doaj-c523b6b3f1aa4a56bc2bc7bb15d53e172020-11-24T21:32:58ZengMDPI AGInternational Journal of Molecular Sciences1422-00672014-10-011510182671828010.3390/ijms151018267ijms151018267tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial PathogensDaniel C. Shippy0Amin A. Fadl1Department of Animal Sciences, University of Wisconsin-Madison, Madison, WI 53706, USADepartment of Animal Sciences, University of Wisconsin-Madison, Madison, WI 53706, USATransfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modification is essential for translational efficiency. Many enzymes have been implicated in the modification of bacterial tRNAs, and these enzymes may complex with one another or interact individually with the tRNA. Approximately, 100 tRNA modification enzymes have been identified with glucose-inhibited division (GidA) protein and MnmE being two of the enzymes studied. In Escherichia coli and Salmonella, GidA and MnmE bind together to form a functional complex responsible for the proper biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm5s2U34) of tRNAs. Studies have implicated this pathway in a major pathogenic regulatory mechanism as deletion of gidA and/or mnmE has attenuated several bacterial pathogens like Salmonella enterica serovar Typhimurium, Pseudomonas syringae, Aeromonas hydrophila, and many others. In this review, we summarize the potential role of the GidA/MnmE tRNA modification pathway in bacterial virulence, interactions with the host, and potential therapeutic strategies resulting from a greater understanding of this regulatory mechanism.http://www.mdpi.com/1422-0067/15/10/18267tRNA modificationGidAMnmEbacterial pathogenesis |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Daniel C. Shippy Amin A. Fadl |
spellingShingle |
Daniel C. Shippy Amin A. Fadl tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial Pathogens International Journal of Molecular Sciences tRNA modification GidA MnmE bacterial pathogenesis |
author_facet |
Daniel C. Shippy Amin A. Fadl |
author_sort |
Daniel C. Shippy |
title |
tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial Pathogens |
title_short |
tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial Pathogens |
title_full |
tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial Pathogens |
title_fullStr |
tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial Pathogens |
title_full_unstemmed |
tRNA Modification Enzymes GidA and MnmE: Potential Role in Virulence of Bacterial Pathogens |
title_sort |
trna modification enzymes gida and mnme: potential role in virulence of bacterial pathogens |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2014-10-01 |
description |
Transfer RNA (tRNA) is an RNA molecule that carries amino acids to the ribosomes for protein synthesis. These tRNAs function at the peptidyl (P) and aminoacyl (A) binding sites of the ribosome during translation, with each codon being recognized by a specific tRNA. Due to this specificity, tRNA modification is essential for translational efficiency. Many enzymes have been implicated in the modification of bacterial tRNAs, and these enzymes may complex with one another or interact individually with the tRNA. Approximately, 100 tRNA modification enzymes have been identified with glucose-inhibited division (GidA) protein and MnmE being two of the enzymes studied. In Escherichia coli and Salmonella, GidA and MnmE bind together to form a functional complex responsible for the proper biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm5s2U34) of tRNAs. Studies have implicated this pathway in a major pathogenic regulatory mechanism as deletion of gidA and/or mnmE has attenuated several bacterial pathogens like Salmonella enterica serovar Typhimurium, Pseudomonas syringae, Aeromonas hydrophila, and many others. In this review, we summarize the potential role of the GidA/MnmE tRNA modification pathway in bacterial virulence, interactions with the host, and potential therapeutic strategies resulting from a greater understanding of this regulatory mechanism. |
topic |
tRNA modification GidA MnmE bacterial pathogenesis |
url |
http://www.mdpi.com/1422-0067/15/10/18267 |
work_keys_str_mv |
AT danielcshippy trnamodificationenzymesgidaandmnmepotentialroleinvirulenceofbacterialpathogens AT aminafadl trnamodificationenzymesgidaandmnmepotentialroleinvirulenceofbacterialpathogens |
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1725955502694727680 |