Twin arginine translocation system in secretory expression of recombinant human growth hormone

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twin arginine translocation system in secretory expression of recombinant human growth hormone

recombinant protein production in e. coli has several advantages over other expression systems. misfolding, inclusion body formation, and lack of eukaryotic post translational modification are the most disadvantages of this system. exporting of correctly folded proteins to the outside of reductive cytoplasmic environment through twin-arginine system could help to pass these limiting steps. two ...

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CONSTRUCTION OF RECOMBINANT PLASMIDS FOR PERIPLASMIC EXPRESSION OF HUMAN GROWTH HORMONE IN ESCHERICHIA COLI UNDER T7 AND LAC PROMOTERS

In order to study the periplasmic expression of human growth hormone (hGH) in Escherichia coli, the related cDNA was inserted in two expression plasmids carrying pelB signal peptide, one with lac bacterial promoter and the other with a bacteriophage T7-based promoter. The recombinant plasmids were moved to TG1 and BL21 strains of E. coli, respectively. To induce the expression systems, IPTG and...

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Twin-arginine translocation pathway in Streptomyces lividans.

The recently discovered bacterial twin-arginine translocation (Tat) pathway was investigated in Streptomyces lividans, a gram-positive organism with a high secretion capacity. The presence of one tatC and two hcf106 homologs in the S. lividans genome together with the several precursor proteins with a twin-arginine motif in their signal peptide suggested the presence of the twin-arginine transl...

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Twin-arginine-dependent translocation of folded proteins.

Twin-arginine translocation (Tat) denotes a protein transport pathway in bacteria, archaea and plant chloroplasts, which is specific for precursor proteins harbouring a characteristic twin-arginine pair in their signal sequences. Many Tat substrates receive cofactors and fold prior to translocation. For a subset of them, proofreading chaperones coordinate maturation and membrane-targeting. Tat ...

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ژورنال

عنوان ژورنال: Research in Pharmaceutical Sciences

سال: 2016

ISSN: 1735-5362

DOI: 10.4103/1735-5362.194871