Acidic Residues on the N-Terminus of Proinsulin C-Peptide Are Important for the Folding of Insulin Precursor.

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概要

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• To investigate the role of C-peptide in the folding of insulin precursor, a series of C-pep-tide mutant proinsulin genes were constructed, overexpressed in Escherichia coli and the proteins purified. Correct disulfide linkages of these proteins were confirmed by both tryptic peptide mapping and insulin receptor binding analyses. In vitro refolding experiments were performed with the purified proteins and showed that mutations on the glycine-rich middle segment of C-peptide, GGGPGAG, and deletion of the C-terminal pentapeptide, EGSLQ, as well as mutations on the two pairs of dibasic residues at the two ends of C-peptide did not significantly affect the refolding yields. However, both alanine replacement mutation and deletion of three highly conserved acidic residues (EAED) at the N-terminus of the C-peptide resulted in serious aggregation during refolding. The results indicate that the highly conserved acidic N-terminal part of C-peptide is very important for insulin precursor folding, and that C-peptide may have some intramolecular chaperone-like function in the folding of insulin precursor.

• 社団法人 日本生化学会の論文

著者

• Tang Jian-guo

  National Laboratory Of Protein Engineering And Plant Genetic Engineering College Of Life Sciences Pe

• Yang Xing-wen

  National Laboratory Of Protein Engineering And Plant Genetic Engineering College Of Life Sciences Pe

• Chen Li-ming

  National Laboratory Of Protein Engineering And Plant Genetic Engineering College Of Life Sciences Pe

• Tang Jian-Guo

  National Laboratory of Protein Engineering and Plant Genetic Engineering College of Life Sciences, Peking University

関連論文

• Effects of Deletion and Shift of the A20-B19 Disulfide Bond on the Structure, Activity, and Refolding of Proinsulin
• Flexibility Exists in the Region of [A6-A11, A7-B7] Disulfide Bonds during Insulin Precursor Folding
• Acidic Residues on the N-Terminus of Proinsulin C-Peptide Are Important for the Folding of Insulin Precursor
• Acidic Residues on the N-Terminus of Proinsulin C-Peptide Are Important for the Folding of Insulin Precursor.

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