Recombinant Protein Stability in Cyanobacteria

نویسندگان

چکیده

The living cell possesses extraordinary molecular and biochemical mechanisms by which to recognize efficiently remove foreign, damaged, or denatured proteins. This essential function has been a barrier the overexpression of recombinant proteins in most expression systems. A notable exception is E. coli proteins, which, however, end-up as inclusion bodies, i.e., cytoplasmic aggregates that are inaccessible cell's proteasome. Fusion constructs protein vectors proved be unparalleled their ability cause substantial accumulation from plants, animals, bacteria, soluble unicellular cyanobacteria. Recombinant levels range 10-20% total cellular can achieved. present work investigated this unique property context stability Synechocystis sp. PCC 6803 developing applying an vivo tobacco etch virus cleavage system with objective separating target heterologous fusion leader sequences. provides new insights about overexpression, stability, exploitation transgenes commercial interest, highly expressed cyanobacterial biofactory. results support notion eukaryotic plant- animal-origin unstable, when free cytosol but stable configuration native protein. Included analysis plant isoprenoid biosynthetic pathway (isoprene synthase, β-phellandrene geranyl diphosphate synthase), human interferon protein, well prokaryotic (tetanus toxin fragment C antibiotic resistance genes kanamycin chloramphenicol). future success synthetic biology approaches cyanobacteria other systems would require enzymes attain product volume, reported paper sets foundation for such enzyme overexpression.

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ژورنال

عنوان ژورنال: ACS Synthetic Biology

سال: 2021

ISSN: ['2161-5063']

DOI: https://doi.org/10.1021/acssynbio.0c00610