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• W2069370078 abstract "Peptidyl-tRNA hydrolase 1 cleaves the ester bond of peptidyl-tRNA thereby recycling peptidyl-tRNAs generated from premature termination of translation and expression of minigenes and short ORFs. Bacterial Pth1 is essential, highly conserved, and has no essential eukaryotic homolog making it a good target for antibacterial development. Herein we describe the cloning of pth1 gene from Bacillus cereus as an N-terminal hexahistidine fusion protein. Solubility was optimized for overexpression in Escherichia coli. Purity greater than 95% was achieved in one chromatography step. Yields greater than 12mg of purified Pth1 per liter of minimal media were achieved and buffer conditions for long-term solubility were determined. Enzymatic activity of Pth1 from B. cereus was confirmed and quantification of Michaelis-Menten parameters reported." @default.
• W2069370078 created "2016-06-24" @default.
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• W2069370078 date "2014-03-01" @default.
• W2069370078 modified "2023-09-26" @default.
• W2069370078 title "Expression, purification, and solubility optimization of peptidyl-tRNA hydrolase 1 from Bacillus cereus" @default.
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• W2069370078 doi "https://doi.org/10.1016/j.pep.2014.01.007" @default.
• W2069370078 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24480186" @default.
• W2069370078 hasPublicationYear "2014" @default.
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