scholarly journals Fluorescent T7 display phages obtained by translational frameshift

2006 ◽  
Vol 34 (20) ◽  
pp. e137-e137 ◽  
Author(s):  
Erik J. Slootweg ◽  
Hans J.H.G. Keller ◽  
Mark A. Hink ◽  
Jan Willem Borst ◽  
Jaap Bakker ◽  
...  
Keyword(s):  
Translational Frameshift

scholarly journals Conserved Translational Frameshift in dsDNA Bacteriophage Tail Assembly Genes

2004 ◽  
Vol 16 (1) ◽  
pp. 11-21 ◽  
Author(s):  
Jun Xu ◽  
Roger W. Hendrix ◽  
Robert L. Duda
Keyword(s):  
Translational Frameshift ◽  
Tail Assembly

scholarly journals Programmed Translational Frameshift in the Bacteriophage P2 FETUD Tail Gene Operon

2002 ◽  
Vol 184 (23) ◽  
pp. 6522-6531 ◽  
Author(s):  
Gail E. Christie ◽  
Louise M. Temple ◽  
Becky A. Bartlett ◽  
Tina S. Goodwin
Keyword(s):  
Gene Cluster ◽  
Sequence Similarity ◽  
Initiation Site ◽  
Translation Initiation Site ◽  
Amino Acid Sequence Similarity ◽  
Reading Frame ◽  
Coding Regions ◽  
Translational Frameshift ◽  
Bacteriophage P2 ◽  
Contractile Tail

ABSTRACT The major structural components of the P2 contractile tail are encoded in the FETUD tail gene operon. The sequences of genes F I and F II, encoding the major tail sheath and tail tube proteins, have been reported previously (L. M. Temple, S. L. Forsburg, R. Calendar, and G. E. Christie, Virology 181:353-358, 1991). Sequence analysis of the remainder of this operon and the locations of amber mutations Eam30, Tam5, Tam64, Tam215, Uam25, Uam77, Uam92, and Dam6 and missense mutation Ets55 identified the coding regions for genes E, T, U, and D, completing the sequence determination of the P2 genome. Inspection of the DNA sequence revealed a new open reading frame overlapping the end of the essential tail gene E. Lack of an apparent translation initiation site and identification of a putative sequence for a programmed translational frameshift within the E gene suggested that this new reading frame (E′) might be translated as an extension of gene E, following a −1 translational frameshift. Complementation analysis demonstrated that E′ was essential for P2 lytic growth. Analysis of fusion polypeptides verified that this reading frame was translated as a −1 frameshift extension of gpE, with a frequency of approximately 10%. The arrangement of these two genes within the tail gene cluster of phage P2 and their coupling via a translational frameshift appears to be conserved among P2-related phages. This arrangement shows a striking parallel to the organization in the tail gene cluster of phage lambda, despite a lack of amino acid sequence similarity between the tail gene products of these phage families.

scholarly journals Fragment-based discovery of a new class of inhibitors targeting mycobacterial tRNA modification

2020 ◽  
Vol 48 (14) ◽  
pp. 8099-8112 ◽  
Author(s):  
Sherine E Thomas ◽  
Andrew J Whitehouse ◽  
Karen Brown ◽  
Sophie Burbaud ◽  
Juan M Belardinelli ◽  
...  
Keyword(s):  
Rapid Development ◽  
Protein Translation ◽  
Mycobacterium Abscessus ◽  
Attractive Potential ◽  
Trna Modification ◽  
Reading Frame ◽  
New Class ◽  
Translational Frameshift ◽  
New Antibiotics

Abstract Translational frameshift errors are often deleterious to the synthesis of functional proteins and could therefore be promoted therapeutically to kill bacteria. TrmD (tRNA-(N(1)G37) methyltransferase) is an essential tRNA modification enzyme in bacteria that prevents +1 errors in the reading frame during protein translation and represents an attractive potential target for the development of new antibiotics. Here, we describe the application of a structure-guided fragment-based drug discovery approach to the design of a new class of inhibitors against TrmD in Mycobacterium abscessus. Fragment library screening, followed by structure-guided chemical elaboration of hits, led to the rapid development of drug-like molecules with potent in vitro TrmD inhibitory activity. Several of these compounds exhibit activity against planktonic M. abscessus and M. tuberculosis as well as against intracellular M. abscessus and M. leprae, indicating their potential as the basis for a novel class of broad-spectrum mycobacterial drugs.

scholarly journals Expression of a Functional Secreted YopN-TyeA Hybrid Protein in Yersinia pestis Is the Result of a +1 Translational Frameshift Event

2004 ◽  
Vol 186 (15) ◽  
pp. 5160-5166 ◽  
Author(s):  
Franco Ferracci ◽  
James B. Day ◽  
Heather J. Ezelle ◽  
Gregory V. Plano
Keyword(s):  
Sequence Analysis ◽  
Yersinia Pestis ◽  
Yersinia Enterocolitica ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Secreted Protein ◽  
Hybrid Protein ◽  
Translational Frameshift ◽  
Chaperone Complex ◽  
Frameshift Event

ABSTRACT YopN is a secreted protein that prior to secretion directly interacts with the cytosolic SycN/YscB chaperone complex and TyeA. This study identifies a secreted YopN-TyeA hybrid protein that is expressed by Yersinia pestis, but not by Yersinia enterocolitica. DNA sequence analysis and site-directed mutagenesis studies demonstrate that the hybrid protein is the result of a +1 translational frameshift event.

scholarly journals Evolutionary repair reveals an unexpected role of the tRNA modification m1G37 in aminoacylation

2021 ◽  
Author(s):  
Ben E Clifton ◽  
Muhammad Aiman Fariz ◽  
Gen-Ichiro Uechi ◽  
Paola Laurino
Keyword(s):  
Experimental Evolution ◽  
Protein Translation ◽  
Trna Modification ◽  
E Coli ◽  
Growth Defects ◽  
Translational Accuracy ◽  
Translational Frameshift ◽  
Mutant Strains ◽  
Trna Methyltransferase

The tRNA modification m1G37, which is introduced by the tRNA methyltransferase TrmD, is thought to be essential for growth in bacteria due to its role in suppressing translational frameshift errors at proline codons. However, because bacteria can tolerate high levels of mistranslation, it is unclear why loss of m1G37 is not tolerated. Here, we addressed this question by performing experimental evolution of trmD mutant strains of E. coli. Surprisingly, trmD mutant strains were viable even if the m1G37 modification was completely abolished, and showed rapid recovery of growth rate, mainly via tandem duplication or coding mutations in the proline-tRNA ligase gene proS. Growth assays and in vitro aminoacylation assays showed that G37-unmodified tRNAPro is aminoacylated less efficiently than m1G37-modified tRNAPro, and that growth of trmD mutant strains can be largely restored by single mutations in proS that restore aminoacylation of G37-unmodified tRNAPro. These results show that inefficient aminoacylation of tRNAPro is the main reason for growth defects observed in trmD mutant strains and that the ProRS enzyme may act as a gatekeeper of translational accuracy, preventing the use of error-prone unmodified tRNAPro in protein translation. Our work shows the utility of experimental evolution for uncovering the hidden functions of essential genes and has implications for the development of antibiotics targeting TrmD.

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