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 ◽  
Author(s):  
H. Taira
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
In Vitro Selection ◽  
Coli Cell ◽  
Translation System ◽  
Free Translation ◽  
Natural Amino Acids ◽  
Selection Of

Wheat Germ Cell-Free Translation System as a Tool for In vitro Selection of Functional Proteins

2002 ◽  
Vol 5 (6) ◽  
pp. 473-480
Author(s):  
Bentham Science Publisher A.N. Alexandrov ◽  
Bentham Science Publisher V.Yu. Alakhov ◽  
Bentham Science Publisher A.I. Miroshnikov
Keyword(s):  
Germ Cell ◽  
Wheat Germ ◽  
In Vitro Selection ◽  
Translation System ◽  
Free Translation ◽  
Selection Of

scholarly journals Chemical aminoacylation of tRNAs with fluorinated amino acids for in vitro protein mutagenesis

2010 ◽  
Vol 6 ◽  
Author(s):  
Shijie Ye ◽  
Allison Ann Berger ◽  
Dominique Petzold ◽  
Oliver Reimann ◽  
Benjamin Matt ◽  
...  
Keyword(s):  
Amino Acids ◽  
Translation System ◽  
Biologically Relevant ◽  
Fluorinated Amino Acids ◽  
Free Translation ◽  
Trna Species ◽  
A Cell ◽  
Protein Environment ◽  
Vitro Protein

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.

Stabilization of mRNA in an Escherichia coli cell-free translation system

FEBS Letters ◽  
1993 ◽  
Vol 321 (2-3) ◽  
pp. 169-172 ◽  
Author(s):  
Ichiro Hirao ◽  
Satoko Yoshizawa ◽  
Kin-ichiro Miura
Keyword(s):  
Escherichia Coli ◽  
Coli Cell ◽  
Translation System ◽  
Free Translation

scholarly journals Convergent In Vivo and In Vitro Selection of Ceftazidime Resistance Mutations at Position 167 of CTX-M-3 β-Lactamase in Hypermutable Escherichia coli Strains

2008 ◽  
Vol 52 (4) ◽  
pp. 1297-1301 ◽  
Author(s):  
Marina N. Stepanova ◽  
Maxim Pimkin ◽  
Anatoly A. Nikulin ◽  
Varvara K. Kozyreva ◽  
Elena D. Agapova ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Typing ◽  
In Vitro Selection ◽  
Resistance Mutations ◽  
Natural Evolution ◽  
E Coli ◽  
Low Activity ◽  
Selection Of

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.

In vitro selection of resistance to pradofloxacin and ciprofloxacin in canine uropathogenic Escherichia coli isolates

2014 ◽  
Vol 174 (3-4) ◽  
pp. 514-522 ◽  
Author(s):  
Xiaoqiang Liu ◽  
Caterina Lazzaroni ◽  
Sherine A. Aly ◽  
Kamoltip Thungrat ◽  
Dawn M. Boothe
Keyword(s):  
Escherichia Coli ◽  
In Vitro Selection ◽  
Uropathogenic Escherichia Coli ◽  
Selection Of ◽  
Selection Of Resistance

scholarly journals CTX-M Expression and Selection of Ertapenem Resistance in Klebsiella pneumoniae and Escherichia coli

2008 ◽  
Vol 53 (2) ◽  
pp. 832-834 ◽  
Author(s):  
Delphine Girlich ◽  
Laurent Poirel ◽  
Patrice Nordmann
Keyword(s):  
Escherichia Coli ◽  
Klebsiella Pneumoniae ◽  
In Vitro Selection ◽  
Gene Frequencies ◽  
Clinical Strains ◽  
Selection Of

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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