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Biology subjects

Di Leo, R.

Publications and source records attributed to Di Leo, R..

2 recordsLinked to original sources

Functional and Structural Characterization of an IclR Family Transcription Factor for the Development of Dicarboxylic Acid Biosensors

Prokaryotic transcription factors (TFs) regulate gene expression in response to small molecules, thus representing promising candidates as versatile small molecule-detecting biosensors valuable for synthetic biology applications. The engineering of such biosensors requires thorough in vitro and in vivo characterization of TF ligand response as well as detailed molecular structure information. In this work we characterize the PcaR TF belonging to the IclR family. We present in vitro functional analysis of PcaRs ligand profile and construction of genetic circuits for the characterization of PcaR as an in vivo biosensor in the model eukaryote Saccharomyces cerevisiae. We report the crystal structures of PcaR in the apo state and in complex with one of its ligands, succinate, which suggests the mechanism of dicarboxylic acid recognition by this TF. This work provides key structural and functional insights enabling the engineering of PcaR for dicarboxylic acid biosensors. Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=50 SRC="FIGDIR/small/550818v1_ufig1.gif" ALT="Figure 1"> View larger version (15K): org.highwire.dtl.DTLVardef@16bcdd2org.highwire.dtl.DTLVardef@95ba9forg.highwire.dtl.DTLVardef@f598borg.highwire.dtl.DTLVardef@1bfe5f2_HPS_FORMAT_FIGEXP M_FIG C_FIG HighlightsO_LIPcaR is an IclR family transcription regulator responsive to dicarboxylic acids C_LIO_LIPcaR was established as an in vivo biosensor in yeast C_LIO_LICrystal structure of PcaR in the apo form was solved C_LIO_LICrystal structure with PcaR in complex with succinate was solved C_LIO_LISequence alignments unveil ligand-binding positions in the IclR family C_LI

synthetic biology↗

Recombinant production of growth factors for application in cell culture

Culturing eukaryotic cells has widespread applications in research and industry, including the emerging field of cell-cultured meat production colloquially referred to as "cellular agriculture". These applications are often restricted by the high cost of growth medium necessary for cell growth. Mitogenic protein growth factors (GFs) are essential components of growth medium and account for upwards of 90% of the total costs. Here, we present a set of expression constructs and a simplified protocol for recombinant production of functionally active GFs, including FGF-2, IGF-1, PDGF-BB and TGF-{beta}1 in Escherichia coli. Using this expression system, we produced soluble GFs from species including bovine, chicken, and fish. Bioactivity analysis revealed orthologs with improved performance compared to commercially available alternatives. We estimated that the production cost of GFs using our methodology will significantly reduce the cost of cell culture medium, facilitating low-cost protocols tailored for cultured meat production and tissue engineering.

cell biology↗