Gene design of signal sequence for effective secretion of protein | Zendy

Y. Tsuchiya | Zendy; Kazuki Morioka | Zendy; Junsuke Shirai | Zendy; Yuichi Yokomizo | Zendy; Kazuo Yoshida | Zendy

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Gene design of signal sequence for effective secretion of protein

Author(s) -

Y. Tsuchiya,

Kazuki Morioka,

Junsuke Shirai,

Yuichi Yokomizo,

Kazuo Yoshida

Publication year - 2003

Publication title -

nucleic acids symposium series

Language(s) - English

Resource type - Journals

eISSN - 1746-8272

pISSN - 0261-3166

DOI - 10.1093/nass/3.1.261

Subject(s) - signal peptide , secretion , recombinant dna , lysozyme , peptide sequence , secretory protein , biology , gene , yeast , peptide , saccharomyces cerevisiae , microbiology and biotechnology , biochemistry

To improve the secretion level of recombinant protein, the gene sequence coded the chicken lysozyme signal peptide (CLSP) connected with human lysozyme (HLY) was altered to substitute the amino acid sequence, and the effect of mutations on secretion of HLY in yeast was elucidated. The effect of mutations on secretion of recombinant HLY was elucidated in yeast. As the result of experiments, it has been shown that the positive charge in the N-terminal region of signal peptide plays an important role in the function of the eukaryotic signal peptide as well as that of prokaryote. This result enable us to design the ideal sequence for effective secretion of recombinant protein. Using such signal sequence containing additional Arginine residues, secretion levels of HLY in yeast were notably increased.

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