This plasmid expresses the 320-residue N-terminal catalytic fragment of Histidyl-tRNA Synthetase from E. coli and contains a N-terminal 6x polyhistidine-tag. It catalyzes both the specific aminoacylation of tRNA and pyrophosphate exchange and shows no mischarging of noncognate tRNAs. Size exclusion chromatography showed that it is monomeric, indicating that the C-terminal domain is essential for maintaining the dimeric structure of the enzyme.
Histidyl-tRNA synthetases attach amino acids to the 3' ends of their cognate transfer RNAs in a two-step reaction catalyzed by ATP. The accuracy of this reaction is crucial for the overall fidelity of protein synthesis.
From the laboratory of Christopher S. Francklyn, PhD, University of Vermont.
Part of The Investigator's Annexe program.
|Gene/insert name:||N-catalytic domain of E.coli Histidyl-tRNA synthetase|
|Fusion Tag(s):||N-terminal 6x His tag|
|Grow in E. coli at 37 C:||Yes|
|Cloning Site 5':||BamHI|
|Cloning Site 3':||HindIII|
|Insert Size:||960 bp|
|Vector Backbone and Size:||pQE30, 3462 bp|
|High or low copy:||High|
|Shipped:||Ambient temperature (Liquid plasmid DNA in water for domestic orders, spotted on filter paper for international orders)|
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