THE SITE-SPECIFIC PROTEOLYSIS OF ESCHERICHIA COLI SIALIC ACID SYNTHASE AT LYS280

2002 ◽  
Author(s):  
Chun-Hung Lin ◽  
Tzann-Shun Hwang ◽  
Chih-Hung Hung ◽  
Chin-Fen Teo
Keyword(s):  
Escherichia Coli ◽  
Sialic Acid ◽  
Site Specific

An Escherichia coli system for assay of Flp site-specific recombination on substrate plasmids

Gene ◽  
1996 ◽  
Vol 180 (1-2) ◽  
pp. 225-227 ◽  
Author(s):  
Michael R. Snaith ◽  
Nigel J. Kilby ◽  
James A.H. Murray
Keyword(s):  
Escherichia Coli ◽  
Site Specific ◽  
Site Specific Recombination

scholarly journals Site-specific DNA cleavage of synthetic NarL sites by an engineered Escherichia coli NarL protein-1,10-phenanthroline cleaving agent

2008 ◽  
Vol 11 (10) ◽  
pp. 2427-2436 ◽  
Author(s):  
Gaoping Xiao ◽  
Daniel L. Cole ◽  
Robert P. Gunsalus ◽  
David S. Sigman ◽  
Chi-Hong B. Chen
Keyword(s):  
Escherichia Coli ◽  
Dna Cleavage ◽  
Site Specific ◽  
Engineered Escherichia Coli

scholarly journals The Site-Specific Recombination System of the Escherichia coli Bacteriophage Φ24B

2020 ◽  
Vol 11 ◽  
Author(s):  
Mohammed Radhi Mohaisen ◽  
Alan John McCarthy ◽  
Evelien M. Adriaenssens ◽  
Heather Elizabeth Allison
Keyword(s):  
Escherichia Coli ◽  
Site Specific ◽  
Site Specific Recombination ◽  
Recombination System ◽  
Site Specific Recombination System

scholarly journals Site-Specific Incorporation of Unnatural Amino Acids into Escherichia coli Recombinant Protein: Methodology Development and Recent Achievement

Biomolecules ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 255 ◽  
Author(s):  
Sviatlana Smolskaya ◽  
Yaroslav Andreev
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Trna Synthetase ◽  
Nonsense Suppression ◽  
Expression Vectors ◽  
Site Specific ◽  
Suppressor Trna ◽  
E Coli ◽  
Orthogonal Pair

More than two decades ago a general method to genetically encode noncanonical or unnatural amino acids (NAAs) with diverse physical, chemical, or biological properties in bacteria, yeast, animals and mammalian cells was developed. More than 200 NAAs have been incorporated into recombinant proteins by means of non-endogenous aminoacyl-tRNA synthetase (aa-RS)/tRNA pair, an orthogonal pair, that directs site-specific incorporation of NAA encoded by a unique codon. The most established method to genetically encode NAAs in Escherichia coli is based on the usage of the desired mutant of Methanocaldococcus janaschii tyrosyl-tRNA synthetase (MjTyrRS) and cognate suppressor tRNA. The amber codon, the least-used stop codon in E. coli, assigns NAA. Until very recently the genetic code expansion technology suffered from a low yield of targeted proteins due to both incompatibilities of orthogonal pair with host cell translational machinery and the competition of suppressor tRNA with release factor (RF) for binding to nonsense codons. Here we describe the latest progress made to enhance nonsense suppression in E. coli with the emphasis on the improved expression vectors encoding for an orthogonal aa-RA/tRNA pair, enhancement of aa-RS and suppressor tRNA efficiency, the evolution of orthogonal EF-Tu and attempts to reduce the effect of RF1.

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