scholarly journals In vitro selection of tRNAs for efficient four-base decoding to incorporate non-natural amino acids into proteins in an Escherichia coli cell-free translation system

2006 ◽  
Vol 34 (5) ◽  
pp. e44-e44 ◽  
H. Taira
2002 ◽  
Vol 5 (6) ◽  
pp. 473-480
Bentham Science Publisher A.N. Alexandrov ◽  
Bentham Science Publisher V.Yu. Alakhov ◽  
Bentham Science Publisher A.I. Miroshnikov

Shijie Ye ◽  
Allison Ann Berger ◽  
Dominique Petzold ◽  
Oliver Reimann ◽  
Benjamin Matt ◽  

This article describes the chemical aminoacylation of the yeast phenylalanine suppressor tRNA with a series of amino acids bearing fluorinated side chains via the hybrid dinucleotide pdCpA and ligation to the corresponding truncated tRNA species. Aminoacyl-tRNAs can be used to synthesize biologically relevant proteins which contain fluorinated amino acids at specific sites by means of a cell-free translation system. Such engineered proteins are expected to contribute to our understanding of discrete fluorines’ interaction with canonical amino acids in a native protein environment and to enable the design of fluorinated proteins with arbitrary desired properties.

FEBS Letters ◽  
1993 ◽  
Vol 321 (2-3) ◽  
pp. 169-172 ◽  
Ichiro Hirao ◽  
Satoko Yoshizawa ◽  
Kin-ichiro Miura

2008 ◽  
Vol 52 (4) ◽  
pp. 1297-1301 ◽  
Marina N. Stepanova ◽  
Maxim Pimkin ◽  
Anatoly A. Nikulin ◽  
Varvara K. Kozyreva ◽  
Elena D. Agapova ◽  

ABSTRACT We report on a novel CTX-M extended-spectrum β-lactamase (ESBL), designated CTX-M-42, with enhanced activity toward ceftazidime. CTX-M-42 was identified in a hypermutable Escherichia coli nosocomial isolate (isolate Irk2320) and is a Pro167Thr amino acid substitution variant of CTX-M-3. By molecular typing of ESBL-producing E. coli strains previously isolated in the same hospital ward, we were able to identify a putative progenitor (strain Irk1224) of Irk2320, which had a mutator phenotype and harbored the CTX-M-3 β-lactamase. To reproduce the natural evolution of CTX-M-3, we selected for ceftazidime resistance mutations in bla CTX-M-3 gene in vitro both in clinical isolate Irk1224 and in laboratory-derived hypermutable (mutD5) strain GM2995. These experiments yielded CTX-M-3Pro167Ser and CTX-M-3Asn136Lys mutants which conferred higher levels of resistance to ceftazidime than to cefotaxime. CTX-M-3Asn136Lys had a level of low activity toward ampicillin, which may explain its absence from clinical isolates. We conclude that the selection of CTX-M-42 could have occurred in vivo following treatment with ceftazidime and was likely facilitated by the hypermutable background.

2014 ◽  
Vol 174 (3-4) ◽  
pp. 514-522 ◽  
Xiaoqiang Liu ◽  
Caterina Lazzaroni ◽  
Sherine A. Aly ◽  
Kamoltip Thungrat ◽  
Dawn M. Boothe

2008 ◽  
Vol 53 (2) ◽  
pp. 832-834 ◽  
Delphine Girlich ◽  
Laurent Poirel ◽  
Patrice Nordmann

ABSTRACT In vitro selection of mutants with decreased susceptibility to ertapenem was performed using Escherichia coli and Klebsiella pneumoniae clinical strains producing either the bla CTX-M-2, bla CTX-M-3, bla CTX-M-9, or bla CTX-M-15 gene. Frequencies of mutants with decreased susceptibilities to ertapenem were similar for all β-lactamases expressed.

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