Expression, purification, and characterization of N-terminal His-tagged proteins with mutations in zinc finger 3 of zinc finger protein ZNF191(243–368)

Zhao, Dongxin; Huang, Zhong‐Xian; Liu, Jie; Ma, Li; He, Juan

doi:10.1080/10826068.2018.1514518

Cited by 1 publication

(1 citation statement)

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“…E. coli encode chaperones, some of which drive the process of protein folding, while others inhibit protein aggregation [ 134 ]. As soon as freshly synthesized proteins detach from the exit site of the E. coli ribosome, they are connected with chaperone with the cause factor [ 140 , 141 ]. Exposed hydrophobic patches on freshly synthesized proteins are shielded from unwanted inter- or intramolecular interactions by associating with the trigger factor, thereby preventing premature folding.…”

Section: Co-expression Of Chaperonesmentioning

confidence: 99%

Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds

Lee

Park

2020

Antibiotics

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Bacteria can produce recombinant proteins quickly and cost effectively. However, their physiological properties limit their use for the production of proteins in their native form, especially polypeptides that are subjected to major post-translational modifications. Proteins that rely on disulfide bridges for their stability are difficult to produce in Escherichia coli. The bacterium offers the least costly, simplest, and fastest method for protein production. However, it is difficult to produce proteins with a very large size. Saccharomyces cerevisiae and Pichia pastoris are the most commonly used yeast species for protein production. At a low expense, yeasts can offer high protein yields, generate proteins with a molecular weight greater than 50 kDa, extract signal sequences, and glycosylate proteins. Both eukaryotic and prokaryotic species maintain reducing conditions in the cytoplasm. Hence, the formation of disulfide bonds is inhibited. These bonds are formed in eukaryotic cells during the export cycle, under the oxidizing conditions of the endoplasmic reticulum. Bacteria do not have an advanced subcellular space, but in the oxidizing periplasm, they exhibit both export systems and enzymatic activities directed at the formation and quality of disulfide bonds. Here, we discuss current techniques used to target eukaryotic and prokaryotic species for the generation of correctly folded proteins with disulfide bonds.

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Section: Co-expression Of Chaperonesmentioning

confidence: 99%