Production of heterologous proteins results in a number of metabolic and physiological changes in the host cells during the course of a production process, namely the induction of stress responses and corresponding alterations in gene expression profiles [1].
Results
This study focuses on quantitative monitoring of the adaptation of E. coli to recombinant protein production on the transcriptome level by a bead-based RNA sandwich hybridisation assay, a rapid novel method based on the detection of hybridisation events between specific oligonucleotide probes and the target nucleic acids [2,3].The expression profiles of selected genes including the product gene, anabolic and stress responsive genes were quantitatively analyzed in cells producing the human basic fibroblast growth factor (hFGF-2), a protein that partially aggregates into inclusion bodies. Transcriptome profiles during temperature- and IPTG-induced synthesis of hFGF-2 using the K12 strain TG1 and BL21(DE3) as production hosts, respectively, were compared.
Authors: M Gabig-Ciminska; A Holmgren; H Andresen; K Bundvig Barken; M Wümpelmann; J Albers; R Hintsche; A Breitenstein; P Neubauer; M Los; A Czyz; G Wegrzyn; G Silfversparre; B Jürgen; T Schweder; S-O Enfors Journal: Biosens Bioelectron Date: 2004-01-15 Impact factor: 10.618
Authors: Jaakko Soini; Christina Falschlehner; Christina Mayer; Daniela Böhm; Stefan Weinel; Johanna Panula; Antti Vasala; Peter Neubauer Journal: Microb Cell Fact Date: 2005-04-01 Impact factor: 5.328